Amyloid-beta peptide crystal structure

ABSTRACT

The invention relates provides a novel crystal structure of the fibrillogenic part of amyloid β-peptide (Aβ). More specifically the crystal structure is Aβ-IgNAR and, accordingly the present invention also relates to selecting and/or designing compounds that modulate amyloid β-peptide (Aβ) activity using techniques such as in silico screening and crystal soaking experiments. The invention further relates to compounds and methods for inhibiting interaction between amyloid β-peptide (Aβ) monomers, more particularly, inhibiting or disrupting amyloid β-peptide (Aβ) oligomer formation and toxic activity.

This application is associated with and claims priority from Australian patent application no. 2008905174 filed on 6 Oct. 2008 and Australian patent application no. 2008905176 filed on 6 Oct. 2008, the entire contents of each of these applications are incorporated herein by reference.

FIELD

The invention relates generally to a novel crystal structure of the fibrillogenic part of amyloid β-peptide (Aβ). More specifically the crystal structure is Aβ-IgNAR and, accordingly the present invention also relates to selecting and/or designing compounds that modulate amyloid β-peptide (Aβ) activity using techniques such as in silico screening and crystal soaking experiments. The invention further relates to compounds and methods for inhibiting interaction between amyloid β-peptide (Aβ) monomers, more particularly, inhibiting or disrupting amyloid β-peptide (Aβ) oligomer formation and toxic activity

BACKGROUND

Bibliographic details of the publications referred to by author in this specification are collected alphabetically at the end of the description. The disclosure of each reference referred to in this application is incorporated herein by reference.

Reference to any prior art in this specification is not, and should not be taken as, an acknowledgment or any form of suggestion that this prior art forms part of the common general knowledge in any country.

Alzheimer's disease (AD) is a progressive neurodegenerative disorder characterized by the presence of misfolded protein depositions or amyloid plaques Crouch, P. J., S.-M. E. Harding, et al. (2008). “Mechanisms of Aβ mediated neurodegeneration in Alzheimer's disease.” Int J Biochem Cell Biol 40(2): 181-198. Plaques consist predominantly of amyloid β-peptide (Aβ), which is produced by cleavage from the membrane-bound amyloid precursor protein (APP) via the β/γ secretase pathway. (The sequence of Aβ is set out in SEQ ID NO 1). However, the current view suggests that soluble Aβ oligomer intermediates, and not the plaque burden, may be the major drivers of Aβ-mediated neuronal dysfunction Walsh, D. M. and D. J. Selkoe (2007). “Aβ oligomers—a decade of discovery.” J. Neurochem. 101(5): 1172-1184. Shankar, G. M., S. Li, et al. (2008). “Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory.” Nat. Med. Frustratingly, obtaining atomic resolution information for Aβ and such oligomers has been a major challenge Kajava, A. V., J. M. Squire, et al. (2006). “β-structures in fibrous proteins.” Adv Protein Chem 73: 1-15. Nelson, R. and D. Eisenberg (2006). “Recent atomic models of amyloid fibril structure.” Curr Opin Struct Biol 16(2): 260-265. Nelson, R. and D. Eisenberg (2006). “Structural models of amyloid-like fibrils.” Adv Protein Chem 73: 235-282, due in part to the propensity of the peptide to form amyloidal fibrils and aggregates rather than form crystallographic lattices.

The present inventors have obtained a 2.2 Å resolution crystal structure of residues 18-41 of Aβ peptide constrained within the CDR3 loop region of a shark IgNAR single variable domain antibody Henderson, K. A., V. A. Streltsov, et al. (2007). “Structure of an IgNAR-AMA1 complex: targeting a conserved hydrophobic cleft broadens malarial strain recognition.” Structure 15(11): 1452-66. The predominant oligomeric species is a tightly-associated Aβ dimer, with paired dimers forming a tetramer which is caged within four IgNAR domains, preventing further uncontrolled amyloid formation. The results reveal unusual Aβ loop topologies and inter-peptide interactions, strikingly different from fibrillar models based on solid state NMR spectroscopy data Petkova, A. T., Y. Ishii, et al. (2002). “A structural model for Alzheimer's b-amyloid fibrils based on experimental constraints from solid state NMR.” Proc Natl Acad Sci USA 99(26): 16742-16747. Luhrs, T., C. Ritter, et al. (2005). “3D structure of Alzheimer's amyloid-β(1-42) fibrils.” Proc Natl Acad Sci USA 102(48): 17342-17347. Petkova, A. T., W. M. Yau, et al. (2006). “Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils.” Biochemistry 45(2): 498-512. Sato, T., P. Kienlen-Campard, et al. (2006). “Inhibitors of amyloid toxicity based on β-sheet packing of Aβ40 and Aβ42.” Biochemistry 45(17): 5503-5516, that describe Aβ residues 18-42 as forming parallel, in-register β-sheets. Notwithstanding, conserved elements can be identified within the structure consistent with residues and motifs previously identified as critical in Aβ peptide folding and neurotoxicity. This crystallographic model suggests a novel paradigm for Aβ oligomer formation, and potentially provides a system for the testing of Aβ oligomer imaging reagents and Alzheimer's disease drug candidates.

SUMMARY OF THE INVENTION

In a first aspect the present invention provides a crystal of amyloid β-peptide (Aβ(18-41) as a fusion with IgNAR (Aβ-IgNAR). In a preferred embodiment the Aβ-IgNAR crystal substantially conforms to the atomic co-ordinates of Appendix I. Preferably at least 75% of the structure has the recited RMSD value, more preferably at least 90% of the structure has the recited RMSD value and most preferably about 100% of the structure has the recited RMSD value.

In a second aspect the present invention provides an Aβ-IgNAR molecule having the amino acid sequence of SEQ ID Nos 15 to 24.

In a third aspect the present invention provides a method of assessing the interaction of a compound with Aβ, the method comprising contacting the crystal of the present invention with the compound and measuring the level of binding of the compound to the Aβ crystal.

In a fourth aspect the present invention provides a method of selecting or designing a compound that interacts with Aβ protein, the method comprising (a) assessing the stereochemical complementarity between a compound and a topographic region of Aβ protein, wherein the protein comprises: (i) amino acids 18-41 of the Aβ protein positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å; or (ii) one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) obtaining a compound which possesses stereochemical complementarity to a topographic region of the Aβ protein; and (c) testing the compound for its ability to modulate an activity associated with the Aβ protein.

In a fifth aspect the present invention provides a method for identifying a potential modulator compound for Aβ protein which method comprises: (a) providing a three-dimensional structure of amino acids 18-41 of Aβ protein as defined by the atomic coordinates shown in Appendix I, or atomic coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) providing the three-dimensional structure of a candidate compound; and (c) assessing the stereochemical complementarity between the three-dimensional structure of step (b) and a topographic region of the three-dimensional structure of step (a).

In a sixth aspect the present invention provides a computer-assisted method for identifying potential compounds able to interact with Aβ protein and thereby modulate an activity mediated by Aβ protein, using a programmed computer comprising a processor, an input device, and an output device, comprising the steps of: (a) inputting into the programmed computer, through the input device, data comprising the atomic coordinates of amino acids 18-41 of Aβ protein as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) generating, using computer methods, a set of atomic coordinates of a structure that possesses stereochemical complementarity to the atomic coordinates of amino acids 18-41 of the Aβ protein as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations, thereby generating a criteria data set; (c) comparing, using the processor, the criteria data set to a computer database of chemical structures; (d) selecting from the database, using computer methods, chemical structures which are similar to a portion of said criteria data set; and (e) outputting, to the output device, the selected chemical structures which are complementary to or similar to a portion of the criteria data set.

In a seventh aspect the present invention provides a method for evaluating the ability of a chemical entity to interact with Aβ protein, said method comprising the steps of: (a) creating a computer model of amino acids 18-41 of Aβ protein using structure coordinates wherein the root mean square deviation between said structure coordinates and the structure coordinates of amino acids 18-41 of Aβ protein as set forth in Appendix I is not more than about 1.5 Å; (b) employing computational means to perform a fitting operation between the chemical entity and said computer model of the binding surface; and (c) analysing the results of said fitting operation to quantify the association between the chemical entity and the Aβ protein model.

In an eighth aspect the present invention provides a computer for producing a three-dimensional representation of a molecule or molecular complex, wherein the computer comprises: (a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein the machine readable data comprise the atomic coordinates of amino acids 18-41 of Aβ protein as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) a working memory for storing instructions for processing the machine-readable data; (c) a central-processing unit coupled to the working memory and to the machine-readable data storage medium, for processing the machine-readable data into the three dimensional representation; and (d) an output hardware coupled to the central processing unit, for receiving the three-dimensional representation.

In a ninth aspect the present invention provides a method of assessing the ability of a compound to affect the ability of Aβ to form dimers or tetramers, the method comprising assessing the level Aβ-IgNAR dimerisation or tetramerisation in the presence or absence of the compound.

In an embodiment of this aspect of the invention the Aβ-IgNAR has the amino acid sequence of any one of SEQ ID NOs: 2, 4-13, 15-24. In another embodiment the assessment of dimerisation or tetramerisation is made by SDS-PAGE or western blot.

In a tenth aspect the present invention provides a method of assessing the affect of a mutation in Aβ to affect the ability of Aβ to form dimers or tetramers, the method comprising assessing the level of dimerisation or tetramerisation of Aβ-IgNAR including the mutation, assessing the level of dimerisation or tetramerisation of Aβ-IgNAR without the mutation and comparing the two levels.

In an embodiment of this aspect of the invention the Aβ-IgNAR not including the mutation has the amino acid sequence of any one of SEQ ID NOs: 2, 4-6, 15-18. In another embodiment the assessment of dimerisation or tetramerisation is made by SDS-PAGE or western blot.

In a eleventh aspect the present invention provides a compound for inhibiting or disrupting amyloid β-peptide oligomer formation or toxic activity, wherein the compound interacts with the region of Aβ-peptide defined by N27, K28, I31 and L34 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.

In an twelfth aspect the present invention provides a compound for inhibiting or disrupting amyloid β-peptide oligomer formation or toxic activity, wherein the compound interacts with the region of Aβ-peptide defined by G33, L34, M35 and V36 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.

In a thirteenth aspect the present invention provides a compound for inhibiting or disrupting amyloid β-peptide oligomer formation or toxic activity, wherein the compound interacts with the region of Aβ-peptide defined by V18, F20, S26, K28, G29, I32, M35, V39 and I41 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.

In a fourteenth aspect the present invention provides a compound for decreasing metal binding by amyloid β-peptide oligomers, wherein the compound interacts with the aligned E22 of the Aβ monomers in the Aβ oligomer.

In a fifteenth aspect the present invention provides the use of an Aβ-IgNAR molecule of any one SEQ ID NOs 2, 4, 5, 6, 13, 15, 16, 17 or 18 to raise antibodies against Aβ wherein the antibodies bind to residues 18 to 41 of SEQ ID NO 1 when presented in the Aβ-IgNAR molecule of any one of SEQ ID NOs 2, 4, 5, 6, 13, 15, 16, 17 or 18 but not to an isolated linear peptide having a sequence of residues 18 to 41 of SEQ ID NO 1.

In a sixteenth aspect the present invention provides an antibody which specifically binds to residues 18 to 41 of SEQ ID NO 1 when presented in the Aβ-IgNAR molecule of any one of SEQ ID NOs 2, 4, 5, 6, 13, 15, 16, 17 or 18 but not to an isolated linear peptide having the sequence of residues 18 to 41 of SEQ ID NO 1.

BRIEF DESCRIPTION OF THE FIGURES

FIG. 1 shows a schematic representation Aβ-IgNAR dimer, illustrating dimer (1), tetramer (2), and amyloid (3) interfaces.

FIG. 2 Aβ-IgNAR fusions form a stable dimer. a, Affinity purified Aβ-IgNAR-G1 elutes as a dimer by gel filtration (solid line) in comparison to 12Y-2 IgNAR monomer (dotted line), b, SDS-PAGE of affinity-purified Aβ-IgNAR-G1 under reducing (R) and non-reducing (U) conditions, illustrating formation of tetrameric (arrowed) species in the absence of heating/reducing agent.

FIG. 3 Representative electron density for Aβ-IgNAR-G1. Electron density 2F₀—F_(c) for residues 18-41 of Aβ-IgNAR-G1 chain A. The map is contoured at 1.0σ.

FIG. 4 Aβ-IgNAR-G1 tetramer. Three aspects of the Aβ-IgNAR-G1 tetramer are shown, illustrating the axis of approximate symmetry through dimeric and tetrameric forms.

FIG. 5 Models of amyloid fibril formation. a, Construction of Aβ oligomer model based on the Aβ-IgNAR-G1 tetramer, incorporating six Aβ (1-41) metal-binding tetramers. The cartoon representation is overlayed with surfaces shaded by chains. Black spheres represent metals (Zn, Cu etc). b, As for a, represented as solubility surface (dark—hydrophilic; light—hydrophobic) c, View along the oligomer axis.

FIG. 6 In silico docking of ChemBridge 9124833 to the Aβ-IgNAR-G1 structure. The compound 3-methoxy-4-[2-(4-morpholinyl)-2-oxoethoxy]aniline (dark shading) docked within the Aβ-IgNAR-G1 structure (wireframe).

FIG. 7 In silico docking of ChemBridge 7996209 to the Aβ-IgNAR-G1 structure. The compound N-[2-(4-methylphenyl)-2-oxoethyl]-1-oxo-3,4-dihydro-1H-isochromene-3-carboxamide (dark shading) docked within the Aβ-IgNAR-G1 structure (wireframe).

FIG. 8 In silico docking of ChemBridge 7949851 to the Aβ-IgNAR-G1 structure. The compound methyl [3-(phenoxyacetyl)-1H-indol-1-yl]acetate (dark shading) docked within the Aβ-IgNAR-G1 structure (wireframe).

FIG. 9 In silico docking of ChemBridge 7780327 to the Aβ-IgNAR-G1 structure. The compound 2-methyl-3-{[(3-methylphenoxy)acetyl]amino}benzoic acid (dark shading) docked within the Aβ-IgNAR-G1 structure (wireframe).

FIG. 10 In silico docking of ChemBridge 7302096 to the Aβ-IgNAR-G1 structure. The compound 3-{[(2,5-dimethoxyphenyl)amino]carbonyl}-7-oxabicyclo[2.2.1]hept-5-ene-2-carboxylic acid (dark shading) docked within the Aβ-IgNAR-G1 structure (wireframe).

FIG. 11 In silico docking of ChemBridge 5785027 to the Aβ-IgNAR-G1 structure. The compound 2-{2-[(2-hydroxyethyl)amino]-1H-benzimidazol-1-yl}-1-(1-naphthyl)ethanone hydrobromide (dark shading) docked within the Aβ-IgNAR-G1 structure (wireframe).

FIG. 12 In silico docking of fenofibrate to the Aβ-IgNAR-G1 structure. Fenofibrate (dark shading) docked within the Aβ-IgNAR-G1 structure (wireframe).

DETAILED DESCRIPTION OF THE INVENTION Definitions

The reference to residue numbers in respect of Aβ is to number residue as in the sequence of Aβ as provided in SEQ ID NO: 1. The residue number is not the number of the residue as it appears in the Aβ-IgNAR molecule.

As used herein, the term “atomic coordinates” refer to a set of values which define the position of one or more atoms with reference to a system of axes.

A structure that “substantially conforms” to a given set of atomic coordinates is a structure wherein at least about 50% of such structure has an RMSD of less than about 1.5 Å for the backbone atoms in secondary structure elements in each domain, and more preferably, less than about 1.3 Å for the backbone atoms in secondary structure elements in each domain, and, in increasing preference, less than about 1.0 Å, less than about 0.7 Å, less than about 0.5 Å, and most preferably, less than about 0.3 Å for the backbone atoms in secondary structure elements in each domain.

Preferably a structure that substantially conforms to a given set of atomic co-ordinates is a structure wherein at least about 75% of such structure has the recited RMSD value, more preferably at least about 90% of such structure has the recited RMSD value, and most preferably, about 100% of such structure has the recited RMSD value.

The above definition of “substantially conforms” can be extended to include atoms of amino acid side chains. As used herein, the phrase “common amino acid side chains” refers to amino acid side chains that are common to both the structure which substantially conforms to a given set of atomic coordinates and the structure that is actually represented by such atomic coordinates.

By the terms “modulate” or “modulating” it is meant that the compound changes an Aβ monomer, dimer, or tetramer by at least 10%. Suitably, a compound modulates Aβ monomer, dimer, or tetramer by decreasing oligomerization or toxicity.

By using the terms “inhibition”/“inhibiting” and/or “disruption”/“disrupting” it is intended to include the concept of “modulate” or “modulating.”

The phrase “decrease oligomerization or toxicity” is intended to encompass partial or complete inhibition of oligomerization or toxicity. The ability of a compound to increase or decrease activity can be assessed by any one of the Aβ oligomerization or toxicity assays described herein.

The term “antibody”, as used herein, broadly refers to any immunoglobulin (Ig) molecule comprised of four polypeptide chains, two heavy (H) chains and two light (L) chains, or any functional fragment, mutant, variant, or derivation thereof, which retains the essential epitope binding features of an Ig molecule. Such mutant, variant, or derivative antibody formats are known in the art. Non-limiting embodiments of which are discussed below.

In a full-length antibody, each heavy chain is comprised of a heavy chain variable region (abbreviated herein as HCVR or VH) and a heavy chain constant region. The heavy chain constant region is comprised of three domains, CH1, CH2 and CH3. Each light chain is comprised of a light chain variable region (abbreviated herein as LCVR or VL) and a light chain constant region. The light chain constant region is comprised of one domain, CL. The VH and VL regions can be further subdivided into regions of hypervariability, termed complementarity determining regions (CDR), interspersed with regions that are more conserved, termed framework regions (FR). Each VH and VL is composed of three CDRs and four FRs, arranged from amino-terminus to carboxy-terminus in the following order: FR1, CDR1, FR2, CDR2, FR3, CDR3, FR4. Immunoglobulin molecules can be of any type (e.g., IgG, IgE, IgM, IgD, IgA and IgY), class (e.g., IgG1, IgG2, IgG 3, IgG4, IgA1 and IgA2) or subclass.

The term “antigen binding domain” or “antigen binding portion” of an antibody, as used herein, refers to one or more fragments of an antibody or protein that retain the ability to specifically bind to an antigen (e.g., IL-12). It has been shown that the antigen-binding function of an antibody can be performed by fragments of a full-length antibody. Such antibody embodiments may also be bispecific, dual specific, or multi-specific formats; specifically binding to two or more different antigens. Examples of binding fragments encompassed within the term “antigen-binding portion” of an antibody include (i) a Fab fragment, a monovalent fragment consisting of the VL, VH, CL and CH1 domains; (ii) a F(ab′)2 fragment, a bivalent fragment comprising two Fab fragments linked by a disulfide bridge at the hinge region; (iii) a Fd fragment consisting of the VH and CH1 domains; (iv) a Fv fragment consisting of the VL and VH domains of a single arm of an antibody, (v) a dAb fragment (Ward et al. 1989 Nature 341 544-6, Winter et al., PCT publication WO 90/05144 A1 herein incorporated by reference), which comprises a single variable domain; and (vi) an isolated complementarity determining region (CDR). Furthermore, although the two domains of the Fv fragment, VL and VH, are coded for by separate genes, they can be joined, using recombinant methods, by a synthetic linker that enables them to be made as a single protein chain in which the VL and VH regions pair to form monovalent molecules (known as single chain Fv (scFv); (see e.g., Bird et al. 1988 Science 242 423-6; Huston et al. 1988 Proc Natl Acad Sci USA 85 5879-83). Such single chain antibodies are also intended to be encompassed within the term “antigen-binding portion” of an antibody. Other forms of single chain antibodies, such as diabodies are also encompassed. Diabodies are bivalent, bispecific antibodies in which VH and VL domains are expressed on a single polypeptide chain, but using a linker that is too short to allow for pairing between the two domains on the same chain, thereby forcing the domains to pair with complementary domains of another chain and creating two antigen binding sites (see e.g., Holliger, P., et al., 1993, Proc. Natl. Acad. Sci. USA 90:6444-6448; Poljak, R. J., et al., 1994, Structure 2:1121-1123). Such antibody binding portions are known in the art (Kontermann and Dubel eds., Antibody Engineering 2001 Springer-Verlag. New York. 790 pp., ISBN 3-540-41354-5).

In a first aspect the present invention provides a crystal of amyloid β-peptide Aβ(18-41) as a fusion with IgNAR (Aβ-IgNAR). In a preferred embodiment the Aβ-IgNAR crystal substantially conforms to the atomic co-ordinates of Appendix I. Preferably at least 75% of the structure has the recited RMSD value, more preferably at least 90% of the structure has the recited RMSD value and most preferably about 100% of the structure has the recited RMSD value.

In a second aspect the present invention provides an Aβ-IgNAR molecule having the amino acid sequence of SEQ ID Nos 15 to 24.

In a third aspect the present invention provides a method of assessing the interaction of a compound with Aβ, the method comprising contacting the crystal of the present invention with the compound and measuring the level of binding of the compound to the Aβ crystal.

In a fourth aspect the present invention provides a method of selecting or designing a compound that interacts with Aβ protein, the method comprising (a) assessing the stereochemical complementarity between a compound and a topographic region of Aβ protein, wherein the protein comprises: (i) amino acids 18-41 of the Aβ protein positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å; or (ii) one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) obtaining a compound which possesses stereochemical complementarity to a topographic region of the Aβ protein; and (c) testing the compound for its ability to modulate an activity associated with the Aβ protein.

In a fifth aspect the present invention provides a method for identifying a potential modulator compound for Aβ protein which method comprises: (a) providing a three-dimensional structure of amino acids 18-41 of Aβ protein as defined by the atomic coordinates shown in Appendix I, or atomic coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) providing the three-dimensional structure of a candidate compound; and (c) assessing the stereochemical complementarity between the three-dimensional structure of step (b) and a topographical region of the three-dimensional structure of step (a).

In a sixth aspect the present invention provides a computer-assisted method for identifying potential compounds able to interact with Aβ protein and thereby modulate an activity mediated by Aβ protein, using a programmed computer comprising a processor, an input device, and an output device, comprising the steps of: (a) inputting into the programmed computer, through the input device, data comprising the atomic coordinates of amino acids 18-41 of Aβ protein as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) generating, using computer methods, a set of atomic coordinates of a structure that possesses stereochemical complementarity to the atomic coordinates of amino acids 18-41 of the Aβ protein as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations, thereby generating a criteria data set; (c) comparing, using the processor, the criteria data set to a computer database of chemical structures; (d) selecting from the database, using computer methods, chemical structures which are similar to a portion of said criteria data set; and (e) outputting, to the output device, the selected chemical structures which are complementary to or similar to a portion of the criteria data set.

In a seventh aspect the present invention provides a method for evaluating the ability of a chemical entity to interact with Aβ protein, said method comprising the steps of: (a) creating a computer model of amino acids 18-41 of Aβ protein using structure coordinates wherein the root mean square deviation between said structure coordinates and the structure coordinates of amino acids 18-41 of Aβ protein as set forth in Appendix I is not more than about 1.5 Å; (b) employing computational means to perform a fitting operation between the chemical entity and said computer model of the binding surface; and (c) analysing the results of said fitting operation to quantify the association between the chemical entity and the Aβ protein model.

In an eighth aspect the present invention provides a computer for producing a three-dimensional representation of a molecule or molecular complex, wherein the computer comprises: (a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein the machine readable data comprise the atomic coordinates of amino acids 18-41 of Aβ protein as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) a working memory for storing instructions for processing the machine-readable data; (c) a central-processing unit coupled to the working memory and to the machine-readable data storage medium, for processing the machine-readable data into the three dimensional representation; and (d) an output hardware coupled to the central processing unit, for receiving the three-dimensional representation.

The Aβ-IgNAR crystal may comprises an Aβ-IgNAR monomer, dimer or tetramer as described in more detail below.

In a preferred embodiment, an A11-IgNAR crystal of the invention has the atomic coordinates set forth in Appendix I. It will be understood by those skilled in the art that atomic coordinates may be varied, without affecting significantly the accuracy of models derived therefrom; thus, although the invention provides a very precise definition of a preferred atomic structure, it will be understood that minor variations are envisaged and the claims are intended to encompass such variations. Preferred are variants in which the root mean square deviation (RMSD) of the x, y and z co-ordinates for all backbone atoms other than hydrogen is less than 1.5 Å (preferably less than 1 Å, 0.7 Å or less than 0.3 Å) compared with the coordinates given in Appendix I. It will be readily appreciated by those skilled in the art that a 3D rigid body rotation and/or translation of the atomic coordinates does not alter the structure of the molecule concerned.

In a highly preferred embodiment, the crystal has the atomic coordinates as shown in Appendix I.

As used herein, the term “atomic coordinates” refer to a set of values which define the position of one or more atoms with reference to a system of axes.

The present invention also provides a crystal structure of an Aβ(18-41) polypeptide (monomer, dimer and tetramer), or a region thereof.

The atomic coordinates obtained experimentally for amino acids 18 to 41 of Aβ-IgNAR are shown in Appendix I. However, a person skilled in the art will appreciate that a set of atomic coordinates determined by X-ray crystallography is not without standard error. Accordingly, any set of structure coordinates for an Aβ-IgNAR polypeptide that has a root mean square deviation of protein backbone atoms of less than 1.5 Å when superimposed (using backbone atoms) on the atomic coordinates listed in Appendix I shall be considered identical.

The present invention also comprises the atomic coordinates of Aβ(18-41) polypeptide (monomer, dimer and tetramer) that substantially conform to the atomic coordinates listed in Appendix I.

A structure that “substantially conforms” to a given set of atomic coordinates is a structure wherein at least about 50% of such structure has an RMSD of less than about 1.5 Å for the backbone atoms in secondary structure elements in each domain, and more preferably, less than about 1.3 Å for the backbone atoms in secondary structure elements in each domain, and, in increasing preference, less than about 1.0 Å, less than about 0.7 Å, less than about 0.5 Å, and most preferably, less than about 0.3 Å for the backbone atoms in secondary structure elements in each domain.

In a more preferred embodiment, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 75% of such structure has the recited RMSD value, and more preferably, at least about 90% of such structure has the recited RMSD value, and most preferably, about 100% of such structure has the recited RMSD value.

In an even more preferred embodiment, the above definition of “substantially conforms” can be extended to include atoms of amino acid side chains. As used herein, the phrase “common amino acid side chains” refers to amino acid side chains that are common to both the structure which substantially conforms to a given set of atomic coordinates and the structure that is actually represented by such atomic coordinates.

The variations in coordinates may be generated due to mathematical manipulations of the structure coordinates. For example, the structure coordinates set forth in Appendix I could be manipulated by crystallographic permutations of the structure coordinates, fractionalisation of the structure coordinates, integer additions or subtractions to sets of the structure coordinates, inversion of the structure coordinates, or any combination thereof.

Alternatively, modification in the crystal structure due to mutations, additions, substitutions, and/or deletions of amino acids, or other changes in any of the components that make up the crystal could also account for variations in structure coordinates.

Various computational analyses are used to determine whether a molecular complex or a portion thereof is sufficiently similar to all or parts of the structure of Aβ-IgNAR and Aβ monomer, dimer and tetramer described above. Such analyses may be carried out in current software applications, such as the Molecular Similarity program of QUANTA (Molecular Simulations Inc., San Diego, Calif.) version 4.1.

The Molecular Similarity program permits comparisons between different structures, different conformations of the same structure, and different parts of the same structure.

Comparisons typically involve calculation of the optimum translations and rotations required such that the root mean square difference of the fit over the specified pairs of equivalent atoms is an absolute minimum. This number is given in angstroms.

Accordingly, structural coordinates of Aβ-IgNAR or Aβ monomer, dimer or tetramer within the scope of the present invention include structural coordinates related to the atomic coordinates listed in Appendix I by whole body translations and/or rotations. Accordingly, RMSD values listed above assume that at least the backbone atoms of the structures are optimally superimposed which may require translation and/or rotation to achieve the required optimal fit from which to calculate the RMSD value.

A three dimensional structure of Aβ-IgNAR or Aβ monomer, dimer or tetramer or region thereof which substantially conforms to a specified set of atomic coordinates can be modelled by a suitable modeling computer program such as MODELER (SalI & Blundell, 1993), as implemented in the Insight II Homology software package (Insight II (97.0), MSI, San Diego), using information, for example, derived from the following data: (1) the amino acid sequence of the Aβ-IgNAR or Aβ monomer, dimer or tetramer polypeptide; (2) the amino acid sequence of the related portion(s) of the protein represented by the specified set of atomic coordinates having a three dimensional configuration; and, (3) the atomic coordinates of the specified three dimensional configuration. A three dimensional structure of Aβ-IgNAR or Aβ monomer, dimer or tetramer polypeptide which substantially conforms to a specified set of atomic coordinates can also be calculated by a method such as molecular replacement, which is described in detail below.

Structure coordinates/atomic coordinates are typically loaded onto a machine readable-medium for subsequent computational manipulation. Thus models and/or atomic coordinates are advantageously stored on machine-readable media, such as magnetic or optical media and random-access or read-only memory, including tapes, diskettes, hard disks, CD-ROMs and DVDs, flash memory cards or chips, servers and the internet. The machine is typically a computer.

The structure coordinates/atomic coordinates may be used in a computer to generate a representation, e.g. an image, of the three-dimensional structure of the Aβ-IgNAR or Aβ monomer, dimer or tetramer crystal which can be displayed by the computer and/or represented in an electronic file.

The structure coordinates/atomic coordinates and models derived therefrom may also be used for a variety of purposes such as drug discovery, biological reagent (binding protein) selection and X-ray crystallographic analysis of other protein crystals.

The three-dimensional structure of Aβ-IgNAR or Aβ monomer, dimer or tetramer provided by the present invention can be used to identify potential target binding sites on Aβ monomer, dimer or tetramers, or derived higher order multimers (i.e. to identify those regions of Aβ involved in oligomerization and/or toxicity and/or disease) as well as in methods for identifying or designing compounds which interact with potential target binding sites of Aβ, e.g. potential modulators/inhibitors of A.

In one embodiment, the target binding site is a region of Aβ involved in oligermisation. Preferred target binding sites comprise one or more of the following domains: the dimerisation domain, the tetramerisation domain, the amyloid formation domain.

In a ninth aspect the present invention provides a method of assessing the ability of a compound to affect the ability of Aβ to form dimers or tetramers, the method comprising assessing the level Aβ-IgNAR dimerisation or tetramerisation in the presence or absence of the compound.

In an embodiment of this aspect of the invention the Aβ-IgNAR has the amino acid sequence of any one of SEQ ID NOs: 2, 4-13, 15-24. In another embodiment the assessment of dimerisation or tetramerisation is made by SDS-PAGE or western blot.

In a tenth aspect the present invention provides a method of assessing the affect of a mutation in Aβ to affect the ability of Aβ to form dimers or tetramers, the method comprising assessing the level of dimerisation or tetramerisation of Aβ-IgNAR including the mutation, assessing the level of dimerisation or tetramerisation of Aβ-IgNAR without the mutation and comparing the two levels.

In a eleventh aspect the present invention provides a compound for inhibiting or disrupting amyloid β-peptide oligomer formation or toxic activity, wherein the compound interacts with the region of Aβ-peptide defined by N27, K28, I31 and L34 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.

In an embodiment of this aspect the region of Aβ-peptide is defined by F19, A21, G25, N27, K28, I31 and L34.

In an embodiment of this aspect of the invention the compound is the peptide 27-NKGAI-31 to compete with formation of the dimer.

In another embodiment of this aspect of the invention the compound is the peptide 27-NKxxIxxL-34 (wherein x is any amino acid) to compete with formation of the dimer with or with out flanking residues.

In another embodiment the compound is an antibody or an antigen binding region thereof which binds Aβ-peptide in the region defined by N27, K28, I31 and L34. The antibody or antigen binding region may bind the Aβ-peptide in the region defined by F19, A21, G25, N27, K28, I31 and L34.

In an twelfth aspect the present invention provides a compound for inhibiting or disrupting amyloid β-peptide oligomer formation or toxic activity, wherein the compound interacts with the region of Aβ-peptide defined by G33, L34, M35 and V36 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.

In an embodiment of this aspect the region of Aβ-peptide is defined by I32, G33, L34, M35 and V36.

In an embodiment of this aspect of the invention the compound is the peptide 33-GLMV-36 to compete for tetramer with or without flanking residues

In another embodiment of this aspect of the invention the compound is the peptide 31-IIGLxV-36 (wherein x is any amino acid) to compete with the formation of the tetramer.

In another embodiment the compound is an antibody or an antigen binding region thereof which binds Aβ-peptide in the region defined by G33, L34, M35 and V36. The antibody or antigen binding region may bind the Aβ-peptide in the region defined by I32, G33, L34, M35 and V36.

In a thirteenth aspect the present invention provides a compound for inhibiting or disrupting amyloid β-peptide oligomer formation or toxic activity, wherein the compound interacts with the region of Aβ-peptide defined by V18, F20, S26, K28, G29, I32, M35, V39 and I41 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.

In an embodiment of this aspect the region of Aβ-peptide is defined by V18, F20, D23, S26, K28, G29, A30, I32, M35, G37, V39 and I41.

In an embodiment of this aspect of the invention the compound is the peptide selected from the group consisting of the peptides 26-SxKG-29, 18-VxF-20, 32-IxxM-35, and 39-VxI-41 each with or without flanking sequences; wherein the peptide competes for formation of amyloid.

In another embodiment the compound is an antibody or an antigen binding region thereof which binds Aβ-peptide in the region defined by V18, F20, S26, K28, G29, I32, M35, V39 and I41. The antibody or antigen binding region may bind the Aβ-peptide in the region defined by V18, F20, D23, S26, K28, G29, A30, I32, M35, G37, V39 and I41.

In a fourteenth aspect the present invention provides a compound for decreasing metal binding by amyloid β-peptide oligomers, wherein the compound interacts with the aligned E22 of the Aβ monomers in the Aβ oligomer.

The compounds of the present invention may also be foldamers or peptidomimetics including peptidomimetics based on β-peptides. More information these classes of compounds can be found in the following references, the disclosure of which is incorporated herein by reference.

-   Ripka, Amy Sa; Rich, Daniel Ha. Peptidomimetic design. Current     Opinion in Chemical Biology. Vol: 2, Issue: 4, 1998 441-452. -   Robinson J A, Demarco S, Gombert F, Moehle K, Obrecht D. The design,     structures and therapeutic potential of protein epitope mimetics.     Drug Discov Today. 2008 Sep. 10. -   Robinson J A. beta-Hairpin Peptidomimetics: Design, Structures and     Biological Activities. Acc Chem. Res. 2008 Apr. 16. -   Appella, D. H.; Christianson, L. A.; Karle, I. L.; Powell, D. R.;     Gellman, S. H. β-Peptide Foldamers: Robust Helix Formation in a New     Family of -Amino Acid Oligomers J. Am. Chem. Soc.; (Communication);     1996; 118(51); 13071-13072. -   Gellman, S. H., “Foldamers: a manifesto”, Acc. Chem. Res 1998,     31(4): 173-180. -   Hill D J, Mio M J, Prince R B, Hughes T S, Moore J S, “A field guide     to foldamers”, Chem. Rev. 2001, 101(12): 3893-4012.

In another aspect the present invention provides a method of inhibiting or disrupting amyloid β-peptide oligomer formation or toxic activity, the method comprising contacting the Aβ-peptide with a compound according to the present invention.

In another embodiment of the present invention the peptides have the same or a similar conformation as they do in the Aβ-peptide. This confirmation is provided by the coordinates amino acids 18-41 of the Aβ protein as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.

The target or binding site is a region of Aβ involved in oligermisation. Preferred target or binding sites comprise one or more of the following domains: the dimerisation domain, the tetramerisation domain, the amyloid formation domain.

A schematic representation of Aβ-IgNAR dimer is shown in FIG. 1. The interfaces which may be targeted include:

The dimer interface (1)

The tetramer interface (2) and

The amyloid interface (3)

Alternatively, the target binding site may comprise one or more amino acids from one or more of the following amino acid sequences:

-   -   (i) amino acids V18-I41;     -   (ii) amino acids F19, A21, G25, N27, K28, G29, I31, L34 (dimer         interface)     -   (iii) amino acids I32, G33, L34, M35, V36 (tetramer interface)     -   (iv) amino acids V18, F20, D23, S26, K28, G29, A30, I32, M35,         G37, V39, I41 (amyloid interface)

A compound may interact with a specified region of Aβ-IgNAR and Aβ monomer, dimer, or tetramer (e.g. an interface) by binding either directly or indirectly to that region. A compound which binds directly, binds to the specified region. A compound which binds indirectly, binds to a region in close proximity to or adjacent to the specified region with the result that it interferes with the ability of the specified region to oligomerise, either antagonistically or agonistically. Such interference may be steric, electrostatic, or allosteric. Preferably, a compound interacts with a specified region of the Aβ-IgNAR and Aβ monomer, dimer, or tetramer by binding directly to the specified region.

Binding can be either by covalent or non-covalent interactions, or both. Examples of non-covalent interactions include electrostatic interactions, van der Waals interactions, hydrophobic interactions and hydrophilic interactions.

When a compound interacts with Aβ-IgNAR and Aβ monomer, dimer, or tetramer, it preferably “modulates” Aβ-IgNAR and AJ monomer, dimer, or tetramer activity respectively. By “modulate” we mean that the compound changes an activity of Aβ-IgNAR and Aβmonomer, dimer, or tetramer by at least 10%. Suitably, a compound modulates Aβ-IgNAR and Aβ monomer, dimer, or tetramer by decreasing oligomerization or toxicity. The phrase “decrease oligomerization or toxicity” is intended to encompass partial or complete inhibition of oligomerization or toxicity. The ability of a candidate compound to increase or decrease activity can be assessed by any one of the Aβ oligomerization or toxicity assays described herein.

As mentioned above one of the assay protocols involves assessment of binding using the actual crystal. Binding of chemical fragments/compounds is assessed by soaking or co-crystallizing such fragments/compounds into crystals provided by the invention and then subjecting these to an X-ray beam and obtaining diffraction data. Difference Fourier techniques are readily applied by those skilled in the art to determine the location within the Aβ-IgNAR and Aβ monomer, dimer, or tetramer structure at which these fragments/compounds bind.

Typically compounds derived from the various screening protocols described herein are subjected to biological testing. There are a number of such test and a useful review is provided in Rahimi, F., Shanmugam, A. & Bitan, G.; Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders. Current Alzheimer research 5, 319-341 (2008) The disclosure of which is incorporated herein by reference.

Other methods involving the use of the crystal or A3-IgNAR protein include:

Assays Utilising the Aβ-IgNAR Protein and Crystals/Structure:

Recombinant Protein Production and SDS-PAGE/Western Blot

-   -   Assessment of dimerisation and tetramerisation of recombinant         Aβ-IgNAR proteins.     -   Analysis of affect of familial/in vitro determined/structurally         predicted/experimentally derived mutations on Aβ-IgNAR folding,         oligomerization, and toxicity.     -   Analysis of action of         peptides/compounds/fragments/metals/antibodies on         oligomerization of Aβ peptide.

An example of this method is shown in FIG. 2 a where the monomer-dimer ratio is used an assay tool ie using ability of compounds to disrupt formation of dimer, and assaying by SDS-PAGE and western blot.

Size Exclusion Chromatography

-   -   Assessment of dimerisation and tetramerisation of recombinant         Aβ-IgNAR proteins.     -   Analysis of affect of familial/in vitro determined/structurally         predicted/experimentally derived mutations on Aβ-IgNAR folding,         oligomerization, and toxicity.     -   Analysis of action of peptides/compounds/fragments/antibodies on         dimerisation and tetramerisation of Aβ-IgNAR.     -   Analysis of action of         peptides/compounds/fragments/metals/antibodies on         oligomerization of Aβ-IgNAR.

BIAcore Biosensor

-   -   Determination of binding affinities for         peptides/compounds/fragments/antibodies targeting the Aβ-IgNAR         structure.

Protein Crystallography

-   -   Analysis of affect of familial/in vitro determined/structurally         predicted/experimentally derived mutations on Aβ-IgNAR structure         and oligomerization.     -   Determination of binding site of         peptides/compounds/fragments/metals/antibodies in the Aβ-IgNAR         structure.

X-Ray Absorption Spectrometry

-   -   Determination of binding sites of metals, stoichiometry and         oxidation state in the Aβ-IgNAR structure using X-ray Absorption         Near-Edge Spectroscopy (XANES) and Extended X-ray Absorption         Fine Structure (EXAFS) methods.

Assaying Derived/Selected Peptides/Compounds/Fragments/Antibodies for Activity

Electron Microscopy

-   -   Analysis of action of         peptides/compounds/fragments/metals/antibodies on         oligomerization of Aβ peptide.

Yeast Cell Toxicity Assays

-   -   Analysis of affect of peptides/compounds/fragments/antibodies on         oligomerization of Aβ peptide in yeast systems.     -   Analysis of action of         peptides/compounds/fragments/metals/antibodies in reducing         Aβ-mediated cellular toxicity in yeast systems.

Neuronal Cell Toxicity Assays

-   -   Analysis of action of         peptides/compounds/fragments/metals/antibodies in reducing         Aβ-mediated cellular toxicity in neuronal cell lines.     -   In vitro neuroprotection (MTT) assay against oligomer-mediated         toxicity

Animal Studies

-   -   Analysis of action of         peptides/compounds/fragments/metals/antibodies in reducing         Aβ-mediated cellular toxicity in animal model systems.

Further information regarding these and other methods which may be usefully applied in the present invention is provided in the following references the disclosures of which is incorporated herein by reference

-   Streltsov, V. A. (2008). “X-ray absorption and diffraction studies     of the metal binding sites in amyloid β-peptide.” Eur Biophys J     37(3): 257-263. -   Streltsov, V. A. and J. N. Varghese (2008). “Substrate mediated     reduction of copper-amyloid-β complex in Alzheimer's disease.” Chem     Commun (Camb)(27): 3169-3171. -   Streltsov, V. A. Titmuss, S. J., Epa, V. C., Barnham, K. J.,     Masters, C. L., Varghese, J. N. (2008). “The structure of the     Amyloid β-peptide high affinity Copper II binding site in     Alzheimer's Disease.” Biophysical Journal. (2008) 95 (7) 3447-3456 -   Caine, J., et al. Alzheimer's Ab fused to green fluorescent protein     induces growth stress and a heat shock response. FEMS Yeast Res 7,     1230-1236 (2007). -   Bharadwaj, P., Waddington, L., Varghese, J. & Macreadie, I. G. A new     method to measure cellular toxicity of non-fibrillar and fibrillar     Alzheimer's Abeta using yeast. J Alzheimers Dis 13, 147-150 (2008). -   Mosmann, T. Rapid colorimetric assay for cellular growth and     survival: application to proliferation and cytotoxicity assays.     Journal of immunological methods 65, 55-63 (1983). -   Maynard C J, Cappai R, Volitakis I, Cherny R A, Masters C L, Li Q X,     Bush A I. Gender and genetic background effects on brain metal     levels in APP transgenic and normal mice: implications for Alzheimer     beta-amyloid pathology. J Inorg Biochem. 2006 May; 100(5-6):952-62. -   Gotz, J., et al. A decade of tau transgenic animal models and     beyond. Brain pathology (Zurich, Switzerland) 17, 91-103 (2007).

Direct binding of compounds to Aβ-IgNAR and Aβ monomer, dimer, or tetramer can also be assessed by Surface Plasmon Resonance (BIAcore) (reviewed in Morton & Myszka, 1998). Here Aβ-IgNAR and Aβ monomer, dimer, or tetramer is immobilized on a CM5 or other sensor chip by either direct chemical coupling using amine or thiol-disulphide exchange coupling (Nice & Catimel, 1999) or by capturing as a fusion protein to an appropriately derivatised sensor surface (Morten & Myszka, 1998). The potential binding molecule (called an analyte) is passed over the sensor surface at an appropriate flow rate and a range of concentrations. The classical method of analysis is to collect responses for a wide range of analyte concentrations. A range of concentrations provides sufficient information about the reaction, and by using a fitting algorithm such as CLAMP (see Morton & Myszka, 1998), rate constants can be determined (Morton & Myszka, 1998; Nice & Catimel, 1999). Normally, the ligand surface is regenerated at the end of each analyte binding cycle. Surface regeneration ensures that the same number of ligand binding sites is accessible to the analyte at the beginning of each cycle.

Incubation periods are selected for optimum activity, but may also be optimized to facilitate rapid high-throughput screening. Normally, between 0.1 and 1 hour will be sufficient. In general, a plurality of assay mixtures is run in parallel with different test agent concentrations to obtain a differential response to these concentrations. Typically, one of these concentrations serves as a negative control, i.e. at zero concentration or below the level of detection.

The basic format of oligomerization and toxicity assays are as follows:

-   -   (i) gel filtration; and western blot/SDS-PAGE     -   (ii) cellular assays     -   (iii) electron microscopy and oligomerization     -   (iv) yeast assays     -   (v) animal studies

The compounds/chemical entities of the present invention may be used to modulate Aβ oligomerization and/or toxicity in cells, by direct binding of the chemical entity to an interface or region of Aβ-IgNAR and Aβ monomer, dimer, or tetramer and/or by an allosteric interaction elsewhere.

Given that Aβ monomer, dimer, or tetramer or oligomerization activity and toxicity is implicated in neuronal disfunction and a range of disorders, the compounds of the present invention may also be used to treat, ameliorate or prevent disorders associated with Alzheimer's disease and/or other amyloidogenic neuropathies.

The compounds which interact with Aβ-IgNAR and Aβ monomer, dimer, or tetramer and in particular to interact with the target interfaces, are useful as agonists or antagonists against the action of Aβ on other yet to be identified ligands. The compounds are useful as assay reagents for identifying other useful ligands by, for example as research tools for further analysis of Aβ oligomerization and as potential therapeutics in pharmaceutical compositions.

Aβ-IgNAR and Aβ monomer, dimer, or tetramer antagonists provided by this invention are potentially useful as therapeutics. For example, compounds are potentially useful as treatments for Alzheimers disease. These antagonists may also be used to detect the presence of Ab dimers in biological samples in particular blood and CSF. In this regard the biological sample is contacted with the compound and the level of binding assessed.

As will be evident to the skilled person, the crystal structures presented herein have enabled, for the first time, the identification of critical regions and conformations of Aβ involved in folding, dimerisation, tetramerisation, and oligermisation leading to fibril formation and toxicity.

Using a variety of known modelling techniques, the crystal structure of the present invention can be used to produce a model for at least part of Aβ monomer, dimer, or tetramer, and higher order oligomers.

As used herein, the term “modelling” includes the quantitative and qualitative analysis of molecular structure and/or function based on atomic structural information and interaction models. The term “modelling” includes conventional numeric-based molecular dynamic and energy minimisation models, interactive computer graphic models, modified molecular mechanics models, distance geometry and other structure-based constraint models.

Molecular modelling techniques can be applied to the atomic coordinates of the Aβ-IgNAR and Aβ monomer, dimer, or tetramer or a region thereof to derive a range of 3D models and to investigate the structure of interfaces and binding sites, such as the binding sites of monoclonal antibodies, nonimmunoglobulin binding proteins and inhibitory peptides.

These techniques may also be used to screen for or design small and large chemical entities which are capable of binding Aβ-IgNAR and Aβ monomer, dimer, or tetramer, their respective interfaces, and affecting oligomerization and toxicity. The screen may employ a solid 3D screening system or a computational screening system.

Such modelling methods are to design or select chemical entities that possess stereochemical complementary to particular regions of Aβ-IgNAR and Aβ monomer, dimer, or tetramer. By “stereochemical complementarity” we mean that the compound or a portion thereof makes a sufficient number of energetically favourable contacts with Aβ as to have a net reduction of free energy on binding.

Such stereochemical complementarity is characteristic of a molecule that matches intra-site surface residues located at

-   -   (i) amino acids V18-I41;     -   (ii) amino acids N27, K28, I31, L34, (dimer interface)     -   (iii) amino acids G33, L34, M35, V36; (tetramer interface)     -   (iv) amino acids V18, F20, S26, K28, G29, I32, M35, V39, I41         (amyloid interface),     -   Or combinations thereof.

Additional intra-site residues include:

-   -   amino acids F19, A21, G25, N27, K28, G29, I31, L34 (dimer         interface)     -   amino acids I32, G33, L34, M35, V36 (tetramer interface) amino         acids V18, F20, D23, S26, K28, A30, I32, M35, G37, V39, I41         (amyloid interface)

By “match” we mean that the identified portions interact with the surface residues, for example, via hydrogen bonding or by non-covalent Van der Waals and Coulomb interactions (with surface or residue) which promote desolvation of the molecule within the site, in such a way that retention of the molecule at the binding site is favoured energetically.

It is preferred that the stereochemical complementarity is such that the compound has a K_(d) for the site of less than 10⁻⁴M, more preferably less than 10⁻⁵M and more preferably 10⁻⁶M. In a most preferred embodiment, the K_(d) value is less than 10⁻⁸M and more preferably less than 10⁻⁹M.

Chemical entities which are complementary to the shape and electrostatics or chemistry of the sites characterised by amino acids positioned at atomic coordinates set out in Appendix I will be able to bind to the regions given above, either independently or in combination and when the binding is sufficiently strong, substantially inhibit oligomerization and/or toxicity.

It will be appreciated that it is not necessary that the complementarity between chemical entities and the site(s) extend over all residues of the site(s) in order to inhibit oligomerization and/or toxicity.

A number of methods may be used to identify chemical entities possessing stereo-complementarity to a region of the Aβ-IgNAR and Aβ monomer, dimer, or tetramer. For instance, the process may begin by visual inspection of potential interface sites, on the computer screen based on the Aβ-IgNAR and Aβ monomer, dimer, or tetramer structures, or region thereof, coordinates in Appendix I generated from the machine-readable storage medium. Alternatively, selected fragments or chemical entities may then be positioned in a variety of orientations, or docked, within an individual binding site of Aβ-IgNAR and Aβ monomer, dimer, or tetramer, as defined supra. Modelling software that is well known and available in the art may be used (Guida, 1994). These include QUANTA and InsightII [Molecular Simulations, Inc., San Diego, Calif., a division of Pharmacopiea, Inc., Princeton, N.J., 1992], SYBYL [Molecular Modeling Software, Tripos Associates, Inc., St. Louis, Mo., 1992]. This modelling step may be followed by energy minimization with standard molecular mechanics force fields such as AMBER (Weiner et al., 1984), and CHARMM (Brooks et al., 1983). In addition, there are a number of more specialized computer programs to assist in the process of selecting the binding moieties of this invention.

Specialised computer programs may also assist in the process of selecting fragments or chemical entities. These include, inter alia:

-   1. GRID (Goodford, 1985). GRID is available from Oxford University,     Oxford, UK. -   2. MCSS (MXXXanker & Karplus, 1991). MCSS is available from     Molecular Simulations, Burlington, Mass. -   3. AUTODOCK (Goodsell & Olsen, 1990). AUTODOCK is available from     Scripps Research Institute, La Jolla, Calif. -   4. DOCK (Kuntz et al., 1982). DOCK is available from University of     California, San Francisco, Calif.

Once suitable chemical entities or fragments have been selected, they can be assembled into a single compound. In one embodiment, assembly may proceed by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of Aβ-IgNAR and Aβ monomer, dimer, or tetramer. This is followed by manual model building using software such as Quanta or Sybyl. Alternatively, fragments may be joined to additional atoms using standard chemical geometry.

The above-described evaluation process for chemical entities may be performed in a similar fashion for chemical compounds.

Useful programs to aid one skilled in the art in connecting the individual chemical entities or fragments include:

-   1. CAVEAT (Bartlett et al., 1989). CAVEAT is available from the     University of California, Berkeley, Calif. -   2. 3D Database systems such as MACCS-3D (MDL Information Systems,     San Leandro, Calif.). This area is reviewed in Martin (1992). -   3. HOOK (available from Molecular Simulations, Burlington, Mass.).

Other molecular modeling techniques may also be employed in accordance with this invention, see, e.g., Cohen et al. (1990) and Navia & Murcko (1992).

There are two preferred approaches to designing a molecule, according to the present invention, that complement the stereochemistry of Aβ-IgNAR and Aβ monomer, dimer, or tetramer. The first approach is to in silico directly dock molecules from a three-dimensional structural database, to the interface site(s), using mostly, but not exclusively, geometric criteria to assess the goodness-of-fit of a particular molecule to the site. In this approach, the number of internal degrees of freedom (and the corresponding local minima in the molecular conformation space) is reduced by considering only the geometric (hard-sphere) interactions of two rigid bodies, where one body (the active site) contains “pockets” or “grooves” that form binding sites for the second body (the complementing molecule).

This approach is illustrated by Kuntz et al. (1982) and Ewing et al. (2001), the contents of which are hereby incorporated by reference, whose algorithm for ligand design is implemented in a commercial software package, DOCK version 4.0, distributed by the Regents of the University of California and further described in a document, provided by the distributor, which is entitled “Overview of the DOCK program suite” the contents of which are hereby incorporated by reference. Pursuant to the Kuntz algorithm, the shape of the interface represented by a site on the Aβ-IgNAR and Aβ monomer, dimer, or tetramer is defined as a series of overlapping spheres of different radii. One or more extant databases of crystallographic data, such as the Cambridge Structural Database System maintained by Cambridge University (University Chemical Laboratory, Lensfield Road, Cambridge, U.K.), the Protein Data Bank maintained by the Research Collaboratory for Structural Bioinformatics (Rutgers University, N.J., U.S.A.), LeadQuest (Tripos Associates, Inc., St. Louis, Mo.), Available Chemicals DXXXectory (Molecular Design Ltd., San Leandro, Calif.), and the NCl database (National Cancer Institute, U.S.A) is then searched for molecules which approximate the shape thus defined.

Molecules identified on the basis of geometric parameters, can then be modified to satisfy criteria associated with chemical complementarity, such as hydrogen bonding, ionic interactions and Van der Waals interactions. Different scoring functions can be employed to rank and select the best molecule from a database. See for example Bohm & Stahl (1999). The software package FlexX, marketed by Tripos Associates, Inc. (St. Louis, Mo.) is another program that can be used in this direct docking approach (see Rarey et al., 1996).

The second preferred approach entails an assessment of the interaction of respective chemical groups (“probes”) with the active site at sample positions within and around the site, resulting in an array of energy values from which three-dimensional contour surfaces at selected energy levels can be generated. The chemical-probe approach to ligand design is described, for example, by Goodford, (1985), the contents of which are hereby incorporated by reference, and is implemented in several commercial software packages, such as GRID (product of Molecular Discovery Ltd., West Way House, Elms Parade, Oxford OX2 9LL, U.K.).

Pursuant to this approach, the chemical prerequisites for a site-complementing molecule are identified at the outset, by probing the active site with different chemical probes, e.g., water, a methyl group, an amine nitrogen, a carboxyl oxygen, or a hydroxyl. Favoured sites for interaction between the active site and each probe are thus determined, and from the resulting three-dimensional pattern of such sites a putative complementary molecule can be generated. This may be done either by programs that can search three-dimensional databases to identify molecules incorporating desired pharmacophore patterns or by programs which use the favoured sites and probes as input to perform de novo design. Suitable programs for determining and designing pharmacophores include CATALYST (including HypoGen or HipHop) (Molecular Simulations, Inc), and CERIUS2, DISCO (Abbott Laboratories, Abbott Park, Ill.) and ChemDBS-3D (Chemical Design Ltd., Oxford, U.K.).

The pharmacophore can be used to screen in silico compound libraries/three-dimensional databases, using a program such as CATALYST (Molecular Simulations, Inc); MACCS-3D and ISIS/3D (Molecular Design Ltd., San Leandro, Calif.), ChemDBS-3D (Chemical Design Ltd., Oxford, U.K.), and Sybyl/3 DB Unity (Tripos Associates, Inc., St. Louis, Mo.).

Databases of chemical structures are available from a number of sources including Cambridge Crystallographic Data Centre (Cambridge, U.K.), Molecular Design, Ltd., (San Leandro, Calif.), Tripos Associates, Inc. (St. Louis, Mo.), Chemical Abstracts Service (Columbus, Ohio), the Available Chemical DXXXectory (MDL Inc), the Derwent World Drug Index (WDI), BioByteMasterFile, the National Cancer Institute database (NCl), and the Maybridge catalogue.

De novo design programs include LUDI (Biosym Technologies Inc., San Diego, Calif.), Leapfrog (Tripos Associates, Inc.), Aladdin (Daylight Chemical Information Systems, Irvine, Calif.), and LigBuilder (Peking University, China).

Once an entity or compound has been designed or selected by the above methods, the efficiency with which that entity or compound may bind to Aβ-IgNAR and Aβ monomer, dimer, or tetramer can be tested and optimised by computational evaluation. An effective Aβ-IgNAR and Aβ monomer, dimer, or tetramer binding compound must preferably demonstrate a relatively small difference in energy between its bound and free states (i.e., a small deformation energy of binding). Thus, the most efficient Aβ-IgNAR and Aβ monomer, dimer, or tetramer binding compound should preferably be designed with a deformation energy of binding of not greater than about 10 kcal/mole, preferably, not greater than 7 kcal/mole. Binding compounds may interact with Aβ-IgNAR and Aβ monomer, dimer, or tetramer in more than one conformation that are similar in overall binding energy. In those cases, the deformation energy of binding is taken to be the difference between the energy of the free compound and the average energy of the conformations observed when the compound binds to the protein.

A compound designed or selected as binding to Aβ-IgNAR and Aβ monomer, dimer, or tetramer may be further computationally optimised so that in its bound state it would preferably lack repulsive electrostatic interaction with the target protein. Such non-complementary (e.g., electrostatic) interactions include repulsive charge-charge, dipole-dipole and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the compound and the protein when the compound is bound to Aβ-IgNAR and Aβ monomer, dimer, or tetramer, preferably make a neutral or favourable contribution to the enthalpy of binding.

Once an Aβ-IgNAR and Aβ monomer, dimer, or tetramer-binding compound has been optimally selected or designed, as described above, substitutions may then be made in some of its atoms or side groups to improve or modify its binding properties. Generally, initial substitutions are conservative, i.e., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. It should, of course, be understood that components known in the art to alter conformation should be avoided. Such substituted chemical compounds may then be analysed for efficiency of fit to Aβ-IgNAR and Aβ monomer, dimer, or tetramer by the same computer methods described in detail above.

Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses include: Gaussian 92, revision C (Frisch, Gaussian, Inc., Pittsburgh, Pa.); AMBER, version 4.0 (Kollman, University of California at San Francisco); QUANTA/CHARMM (Molecular Simulations, Inc., Burlington, Mass.); and Insight II/Discover (Biosysm Technologies Inc., San Diego, Calif.).

The screening/design methods may be implemented in hardware or software, or a combination of both. However, preferably, the methods are implemented in computer programs executing on programmable computers each comprising a processor, a data storage system (including volatile and non-volatile memory and/or storage elements), at least one input device, and at least one output device. Program code is applied to input data to perform the functions described above and generate output information. The output information is applied to one or more output devices, in known fashion. The computer may be, for example, a personal computer, microcomputer, or workstation of conventional design.

Each program is preferably implemented in a high level procedural or object-oriented programming language to communicate with a computer system. However, the programs can be implemented in assembly or machine language, if desired. In any case, the language may be compiled or interpreted language.

Each such computer program is preferably stored on a storage medium or device (e.g., ROM or magnetic diskette) readable by a general or special purpose programmable computer, for configuring and operating the computer when the storage media or device is read by the computer to perform the procedures described herein. The system may also be considered to be implemented as a computer-readable storage medium, configured with a computer program, where the storage medium so configured causes a computer to operate in a specific and predefined manner to perform the functions described herein.

Screening Assays and Confirmation of Binding and Biological Activity

Compounds selected or designed in accordance with the in silico methods of the invention may be subjected to further confirmation of binding to Aβ-IgNAR and Aβ monomer, dimer, or tetramer by cocrystallization of the compound with Aβ-IgNAR and Ap monomer, dimer, or tetramer and structural determination, as described herein.

Libraries may be screened in solution by methods generally known in the art for determining whether ligands competitively bind at a common site. Such methods may include screening libraries in solution (e.g.; Houghten, 1992), or on beads (Lam, 1991), chips (Fodor, 1993), bacteria or spores (U.S. Pat. No. 5,223,409: Lardner), plasmids (Cull et al., 1992), or on phage (Scott & Smith, 1990; Devlin, 1990; CwXXXla et al., 1990; Felici, 1991; U.S. Pat. No. 5,223,409: Lardner).

Where the screening assay is a binding assay, Aβ-IgNAR and Aβ monomer, dimer, or tetramer may be joined to a label, where the label can directly or indirectly provide a detectable signal. Various labels include radioisotopes, fluorescent molecules, chemiluminescent molecules, enzymes, specific binding molecules, particles, e.g., magnetic particles, and the like. Specific binding molecules include pairs, such as biotin and streptavidin, digoxin and antidigoxin, etc. For the specific binding members, the complementary member would normally be labeled with a molecule that provides for detection, in accordance with known procedures.

A variety of other reagents may be included in the screening assay. These include reagents like salts, neutral proteins, e.g., albumin, detergents, etc., which are used to facilitate optimal protein-protein binding and/or reduce non-specific or background interactions. Reagents that improve the efficiency of the assay, such as protease inhibitors, nuclease inhibitors, antimicrobial agents, etc., may be used. The components are added in any order that produces the requisite binding. Incubations are performed at any temperature that facilitates optimal activity, typically between 4 and 40° C.

The Aβ-IgNAR molecule may be used in its own right as a sink or tool to mop up oligomers both in vivo and in vitro ie as a therapeutic.

The Aβ-IgNAR molecule of the present invention may also be used as an antigen to raise antibodies against Aβ.

In a fifteenth aspect the present invention provides the use of an Aβ-IgNAR molecule of any one SEQ ID NOs 2, 4, 5, 6, 13, 15, 16, 17 or 18 to raise antibodies against Aα wherein the antibodies bind to residues 18 to 41 of SEQ ID NO 1 when presented in the Aβ-IgNAR molecule of any one of SEQ ID NOs 2, 4, 5, 6, 15, 16, 17 or 18 but not to an isolated linear peptide having a sequence of residues 18 to 41 of SEQ ID NO 1.

In a sixteenth aspect the present invention provides an antibody which specifically binds to residues antibodies bind to residues 18 to 41 of SEQ ID NO 1 when presented in the Aβ-IgNAR molecule of any one of SEQ ID NOs 2, 4, 5, 6, 13, 15, 16, 17 or 18 but not to an isolated linear peptide having a sequence of residues 18 to 41 of SEQ ID NO 1.

In a preferred embodiment the antibody is a monoclonal antibody.

As will be understood by persons skilled in the art the antibodies of the present invention are directed to conformational epitopes of 18-41 of Aβ which are presented when Aβ 18-41 is positioned within the Aβ-IgNAR molecule. Such conformational epitopes will not be present in the isolated linear Aβ 18-41 peptide.

In addition to therapeutic uses the antibodies of the present invention may also be used in diagnostic assays to detect the presence of Aβ dimers in biological samples in particular blood and CSF. In this regard the biological sample is contacted with the antibody and the level of binding assessed.

Throughout this specification the word “comprise”, or variations such as “comprises” or “comprising”, will be understood to imply the inclusion of a stated element, integer or step, or group of elements, integers or steps, but not the exclusion of any other element, integer or step, or group of elements, integers or steps.

All publications mentioned in this specification are herein incorporated by reference. Any discussion of documents, acts, materials, devices, articles or the like which has been included in the present specification is solely for the purpose of providing a context for the present invention. It is not to be taken as an admission that any or all of these matters form part of the prior art base or were common general knowledge in the field relevant to the present invention as it existed in Australia or elsewhere before the priority date of each claim of this application.

In order that the nature of the present invention may be more clearly understood, preferred forms thereof will now be described with reference to the following non-limiting examples.

Example 1 Methods Summary

Construction of Aβ-IgNAR chimeras. Aβ-IgNAR-G1/G3/G6 and G1-Leu³⁴Pro coding sequences were constructed by splice-overlap PCR using IgNAR 12Y-2 DNA template(Nuttall, Humberstone et al. 2004), cloned into E. coli periplasmic expression vector pGC, and verified by DNA sequencing.

Protein purification and crystallization. Recombinant proteins were expressed into the E. coli periplasmic space, purified by affinity chromatography through an anti-FLAG Ig/Sepharose column equilibrated in TBS, and collected as single peaks by gel filtration. Proteins (˜4-5 mg/ml in 20 mM Tris.HCl, pH 8.0) were set up as 0.4 μl sitting drops. Aβ-IgNAR-G1 (SEQ ID NO: 2) crystallised under a wide range of conditions (biased towards PEG 6000; PEG 3350; and PEG MME 2000 at neutral pH). Final crystallisation conditions were 0.2 M ammonium chloride, 20% polyethylene glycol (PEG) 6000, 0.1 M MES pH 6, with diffraction quality crystals (Space Group P3₂ and cell parameters a=b=79.40, c=84.89 Å) obtained after 9 days. No crystals were obtained for Aβ-IgNAR-G3 (SEQ ID NO: 4) or Aβ-IgNAR-G6 (SEQ ID NO: 5).

Structure determination. A full data set (93% completeness) was collected at the Australian Synchrotron 3-BM1 beam line to 2.2 Å resolution. Data were collected at −160° C. and processed using the HKL2000 suite (Otwinowski and Minor 1997). Diffraction data statistics are summarized in Table 1. The structure was solved by molecular replacement MOLREP (Vagin and Teplyakov 1997) using IgNAR 12Y-2 (PDB 1 VES) minus CDR3 region as search template. Four independent molecules (A, B, C and D) were found in the asymmetric unit. The final refinement converged to R/R_(free) values of 0.164/0.246. In total, 97.8% residues are in the most favoured regions of the Ramachandran plot, with 1.6% residues in the additionally allowed regions.

TABLE 1 X-ray refinement statistics Resolution (Å) 26.17-2.20 R_(work)/R_(free) 16.4/24.6 Number of Protein amino acids 503 Water 394 B-factors Overall 46.5 Protein 46.0 Water 51.7 R.m.s deviations Bond lengths (Å) 0.019 Bond angles (°) 1.958

Results

The crystallographic structures of the IgNAR single variable domain antibody 12Y-2(Streltsov, Varghese et al. 2004) (PDB: 1 VES) reveal self-stabilized extended β-hairpin CDR3 loop regions. We hypothesized that engineering the amyloidogenic component of Aβ peptide (residues Val¹⁷-Ala⁴²) within this loop would (1) allow formation of an amyloid protofilament structure; while (2) preventing uncontrolled fibril formation and polymerisation by trapping the amyloid moiety in a cage of IgNAR domains that are amenable to crystallization. Three chimeric proteins were modelled based on existing NMR β-hairpin models of amyloid plaques (Luhrs, Ritter et al. 2005), incorporating variable N- and C-terminal glycine linkers to allow in-register transition from the immunoglobulin framework β-sheets to the Aβ peptide. These constructs, designated Aβ-IgNAR-G1 (SEQ ID NO. 2); Aβ-IgNAR-G3 (SEQ ID NO. 4); and Aβ-IgNAR-G6 (SEQ ID NO. 5), were expressed as recombinant proteins in E. coli and tested for oligomer formation. SDS and β-mercaptoethanol-stable dimers were observed in the bacterial periplasmic space by Western blot for all three chimeric proteins but not the unmodified IgNAR. The greater conformational flexibility for the glycine-3 and glycine-6 versions appeared to allow more rapid dimer formation, and protein induction at higher temperature tended to promote a higher dimer:monomer ratio. Upon affinity purification all 3 variants behaved as dimers, rather than the monomer observed for the wild type IgNAR, and tetrameric species were also apparent. (FIGS. 2 a and 2 b). Trigonal crystals of Aβ-IgNAR-G1 (SEQ ID NO: 2), but not the other two chimeric proteins, grew under a variety of conditions and diffracted to 2.2 Å resolution. The structure was solved by molecular replacement using IgNAR 12Y-2 (SEQ ID NO: 3) with removed CDR₃ region as the search model, and refinement completed with R/R_(free) factors of 16.4/24.6% (Table 1). Representative regions of electron density are shown in FIG. 3.

The Aβ-IgNAR-G1 (SEQ ID NO: 2) quaternary structure consists of four independent molecules (A, B, C and D) in the asymmetric unit (FIG. 4), which form a tight tetramer (dimer of dimers) through interactions predominantly mediated by the Aβ peptide component. The inter-chain association for each dimer (A-C and B-D) is extremely robust, as indicated by an average surface of interaction (buried surface) of 580 Å² and an average shape correlation statistic (Lawrence and Colman 1993) (S_(c))=0.64 (Tables 2 & 3). The dimer-dimer interaction (AC-BD) which forms the crystallographic tetramer is somewhat less extensive (buried surface of 546 Å²). The underlying IgNAR scaffold monomers are very closely overlaid with each-other and with the previously described 12Y-2 structure.

TABLE 2 Aβ-IgNAR-G1 buried surface areas¹. Chain A B C D Total² A — 215.7 589.0 290.8 1095.5 B 215.7 — 254.9 563.8 1034.4 C 578.2 250.2 — 215.8 1044.2 D 296.5 569.6 221.5 — 1087.6 Average 1065.4 ¹For Aβ regions only. ²Area excluded on first molecule due to interaction with second (in Angstroms squared). Calculated using point density = 10 points/square Å; Probe sphere radius = 1.7 Å.

TABLE 3 Aβ-IgNAR-G1 shape complementarity statistics¹. Sc A B C D A 1 0.590 0.709 0.786 B 1 0.742 0.567 C 1 0.717 D 1 ¹Calculated using the Sc program with a 1.7 Å probe radius.

The Aβ-IgNAR-G1 structure reveals the Aβ peptide region (Val¹⁸-Ile⁴¹) as comprising two adjacent and connected loop motifs, rather than the expected extended β-hairpin structure. The first motif consists of residues Val¹⁸-Ile³¹ which adopt a 10-11 Å wide β-α structure, stabilised by intra-molecular and inter-molecular contacts and consisting of one β strand (Val¹⁸-Ala²¹) plus a 3₁₀— helical turn (Val²⁴-Ser²⁶)(chains A) and similar but distorted helix in chain B or an extended loop (chains C and D). The second motif consists of residues Ile³²-Ile⁴¹ and is a β-hairpin consisting of two anti-parallel β-strands which form a 3-strand β-sheet with the parallel β-strand of the first loop motif. The overlaid Aβ loops have an average r.m.s.d.=1.19 Å², and as can be seen from FIG. 2 d the greatest divergence occurs between residues Val²⁴-Asn²⁷, where chains A and B adopt a different conformation from chains C and D. Consequently, for the A/B chain conformations the Lys²⁸ side-chain is directed out of the plane of the loop and forms intramolecular contacts with Val²⁴ (2.6 Å) and Asn²⁷ (3.6 Å) (chain A) and helps maintain the helical conformation of Val²⁴-Ser²⁶. In contrast, for the C/D chains the Lys²⁸ side chain is now directed internally and forms two intra-molecular contacts with the carbonyl oxygens of Asp²³ (3.0 and 3.5 Å) and Ser²⁶ (4.0 and 3.0 Å) and two inter-molecular contacts with carbonyl oxygens of chain A/B: Gly²⁹ (2.6 and 3.3 Å) and Asn²⁷ (2.8 and 3.6 Å). The transition between the two states for Lys²⁸ appears pivotal to crystallisation, and may represent a vital mechanism (and energy minimum) for Aβ oligomer formation. In NMR-based structures of amyloid plaques, residues Leu¹⁷-Ala⁴² form parallel, in-register β-sheets (Petkova, Ishii et al. 2002; Luhrs, Ritter et al. 2005; Sato, Kienlen-Campard et al. 2006), with Lys²⁸ facing outward in the first Aβ chain of the adjacently stacked peptides, while subsequent Aβ peptides have the Lys²⁸ side-chain directed internally and forming intermolecular contacts (salt bridges) with residue Asp²³ (Luhrs, Ritter et al. 2005; Petkova, Yau et al. 2006; Sato, Kienlen-Campard et al. 2006). Thus our structure is consistent with NMR data for this position.

Overall, the dimers (AC and BD), each related by an pseudo 2-fold axis running through the long axis of the tetramer, are stabilized around the Asp²³-Ala³⁰ loop by the carbonyl oxygen charges neutralizing the buried Lys²⁸ amide group and by the amide group of Asp²⁷ forming a hydrogen bonding network with the neighbouring dimer's carbonyl oxygen of Gly²⁹ and carboxy oxygen of Asp²⁷. The surface towards the tetramer interface is stabilized by the hydrophobic residues Ile³¹, Val⁴⁰, and Leu³⁴. The tetramer interface is stabilized by two 3-stranded β-sheets of the monomer forming a single 6-stranded β-sheet with a pseudo-2-fold axis running perpendicular to and through the centroid of the extended β-sheets. The Leu³⁴ side-chains face each other: two from each side of the tetramer, rotated by ˜90° (see later). Similarly, the respective Met³⁵ side-chains are surrounded by hydrophobic residues Ile³², Val³⁹ and Ile⁴¹. Intermolecular contacts seen by NMR such as Ala²¹/Val³⁶ (Luhrs, Ritter et al. 2005) and Ile³²/Leu³⁴/Val³⁶ (Petkova, Yau et al. 2006) are also observed for this motif. An earlier crystallographic structure of Aβ(28-42) fused C-terminally to Tk-RNase HII (Takano, Endo et al. 2006) also suggested formation of a limited β-hairpin conformation which partially overlaps with the Aβ-IgNAR-G1 β-hairpin motif (r.m.s.d.=1.9 Å for 13 atoms).

The tetrameric structure displays features described for various models of both aβ protofilaments (Malinchik, Inouye et al. 1998; Losic, Martin et al. 2006) and soluble globulomers (Barghorn, Nimmrich et al. 2005) and shows strong correlation with other independently obtained structural data for Aβ fragments and fibrils (Rahimi, Shanmugam et al. 2008). The top and bottom of the tetramer is covered by a contiguous hydrophobic surface with a girdle of hydrophilic residues (²²EDVGSNKGA³⁰) running along the sides. The wedged-shape interface visible in our structure also suggest a possible mechanism for membrane-spanning pore formation (Jang, Zheng et al. 2008). Thus, we hypothesised that the observed dimer or tetramer may be a common structural motif in Aβ oligomerization, and modelled the Aβ tetramers minus the IgNAR domain as a building block of high order oligomers. By aligning Aβ tetramers on top of each other along the polar axis, utilising the interaction pattern observed between parallel Aβ stacks by NMR structure (Petkova, Yau et al. 2006), a series of multimeric constructs were generated (FIG. 5 a-c). Sequential tetramers in this model are rotated by ˜30° along the oligomer axis creating a twisted (coiled) cylinder up to ˜40 Å wide. While the N-terminal residue Val¹⁸ appears to be too close to the next tetramer in this configuration, this probably results from constraints imposed by the IgNAR scaffold, which would be absent in a soluble oligomeric form. Adding N-terminal Aβ peptides residues Ala¹-Lys¹⁶, as described by XAFS data (Streltsov 2008), onto the crystallographic tetramer results in a model whereby this unstructured metal-binding fragment is ideally oriented to mediate reactive oxygen species toxicity. Mechanistically, neighbouring tetramers as shown in FIG. 3 a-c align Glu²² and Asp²³ side chains (from different tetramers) to form a belt of 4 potential metal-binding sites (Glu²²-Glu²²=10-12 Å; Asp²³-Asp²³=5.5-7 Å). With contributions from oxygen and nitrogens atoms this may conceivably produce one additional low affinity binding site per A0 monomer in the aggregate. Upon metal binding to the Aβ N-terminus (Asp¹; Glu¹¹; His⁶; His¹³; His¹⁴), the adjacent Val¹⁸-Ala²¹ fragment should be stabilized, facilitating tetramer-tetramer interactions and accelerating oligomer (fibril) growth.

Familial and in vitro-generated mutations represent valuable tools for dissecting Aβ peptide function. For example the major pathogenic familial Aβ mutations (Walsh 2005), i.e. Ala²¹Gly (Flemish), Glu²²Gly (Arctic), Glu²²Lys (Italian) and Asp²³Asn (Iowa) are localized within a β-turn stabilized by hydrogen bonds between Asp²³ (OD1) and Ser²⁶ (OG) (2.8 Å), and Asp²³ (OD2) and Gly²⁵ (N) (3.4 Å). Interactions with Phe²⁰ also appear important for loop stability: Asp²³ (OD1) is at 2.6 Å from an intra-loop water molecule which is at 3.1 Å from Phe²⁰ (N), an interaction which FAD mutation Asp²³Asn is predicted break. Similarly, the “Wurth” mutations (Wurth, Guimard et al. 2002), derived in vitro from studies of the folding of Aβ(1-42)-GFP fusions (Wurth, Guimard et al. 2002), signpost residues important in aggregation. These mutations map into the surface residues of the monomer that interfere with formation of the dimer or tetramer interfaces and the amylogenic surface. For example mutation Leu³⁴Pro is described to markedly decrease Aβ aggregation, both alone and in combination with other variants. Here, the four Leu³⁴ side-chains form a universal type joint, leading to our prediction that a Leu³⁴Pro substitution would here (1) disrupts the central hydrophobic core of the tetramer; and (2) break the β-sheets formed by residues Ile³²-Val³⁶ between adjacent dimers. To test this theory, we produced the variant Aβ-IgNAR-G1 (Leu³⁴Pro) (SEQ ID NO. 7) and assessed the affect of this change on dimerisation. We observed marked reversion to monomeric form, of similar magnitude (˜30%) to that originally described for this mutation in vitro (Wurth, Guimard et al. 2002). Upon affinity purification, this variant tended toward dimerisation, but in contrast to the parental Aβ-IgNAR-G1 was not resistant to β-mercaptoethanol treatment and failed to crystallise, suggesting that the tetramer interface had indeed been compromised.

The mechanistic basis of Aβ-mediated toxicity remains controversial and unresolved. Currently popular candidate mechanisms include: neuronal damage mediated by reactive oxygen species (ROS)(Bush 2000; Streltsov 2008); membrane destabilisation and/or pore formation (Jang, Zheng et al. 2008); and activation or modification of the apotopic pathway (Culmsee and Landshamer 2006). Most probably the final disease aetiology will prove to be multi-factorial. By developing a crystallographic model for amyloidogenic Aβ, we hoped to devise a system to test such hypotheses. Surprisingly, our structures revealed not the expected β-turn-β extended loop, but rather an unusual and compact four-lobed cloverleaf structure, which may prove to be the proto-oligomeric building block. To the best of our knowledge, this “cloverleaf” model is the first full x-ray crystallographic structure of the amyloidogenic component of the Aβ peptide.

Simplistically, our structure can be envisaged as presenting three aspects, which we describe as the dimer interface, the tetramer interface, and the amyloid-extension face. Each potentially represents a viable target for interventionist agents aimed at disrupting oligomer formation and toxic activity. Such moieties may extend beyond imaging agents to novel chemical and biological entities, including chemical compounds and peptidomimetic constructs. In this sense, we believe our structure represents a possible novel paradigm for Aβ folding, which will engender testable hypotheses for the protein folding and toxicity of this medically important peptide and its associated forms.

Example 2 Familial Mutations

A series of variants for Aβ-IgNAR-G1 were produced (Table 4), with the aim of determining the affect of so-called “familial mutations” upon the Aβ-IgNAR-G1 structure. All these mutation map to residues 21-23. All variants displayed the characteristic Aβ dimerization predicted from the structure.

TABLE 4 Protein Description Mutation MW (Da) Tag SEQ ID NO: 35A-1 Aβ-IgNAR — 15,654 FLAG × 2 2 12Y-2 IgNAR wt — 14,878 FLAG × 2 3 37A-1 Aβ-IgNAR Gly3 15,953 FLAG × 2 4 37Q-6 Aβ-IgNAR Gly6 16,123 FLAG × 2 5 37P-3 Aβ-IgNAR Gly2 15,768 FLAG × 2 6 37D-4 Aβ-IgNAR Leu34Pro 15,638 FLAG × 2 7 37F-2 Aβ-IgNAR Asp23Asn 15,653 FLAG × 2 8 37K-1 Aβ-IgNAR Glu22Gln 15,653 FLAG × 2 9 37L-2 Aβ-IgNAR Ala21Gly 15,640 FLAG × 2 10 37R-1 Aβ-IgNAR ΔGlu22 15,525 FLAG × 2 11 37M-4 Aβ-IgNAR Ser26Cys 15,670 FLAG × 2 12 37V-2 Aβ-IgNAR — 14,345 His 13 37Y-1 IgNAR wt — 13,553 His 14

A Western blot showed the characteristic dimerization for the familial mutants compared to wild type Aβ-IgNAR-G1 (35A-1) and the non-dimerizing wild type IgNAR (12Y-2) and “Wurth” mutant 37D-4. Familial mutants of Aβ-IgNAR-G1 reveal the presence of dimeric species at ˜30 kDa, in contrast to the wild type IgNAR (12Y-2) and the mutant Leu34Pro (37D-4)

Example 3 In Silico Screening

The crystallographic structure co-ordinates were taken and screened in silico against a database of compounds.

The crystal structure of the tetramer was examined disregarding the IgNAR domains. A site (cavity) on the ‘amyloidogenic’ surface, bounded by residues (chain B and chain C and Aβ amino acid residue number within these chains) B18, B32, B33, B34, B35, B41, C18, C32, C33, C34, C35, and C41 was selected as the target for docking molecules from the chemical database. The ‘Clean lead-like’ subset (approx. 1136000 compounds) from the ZINC database (http://zinc.docking.org; J. J. Irwin and B. K. Shoichet, J. Chem. Inf. Model. (2005), 45, 177-182) was used for the virtual screening or docking.

First, the program DOCK v. 6.2 (Univ. of California at San Francisco, USA; T. J. A. Ewing et al., J. Comput.-Aided Molec. Design, (2001), 15, 411-428.) was used to dock a segment of approx. 25000 compounds (molecules) from the database to the selected docking site on the tetramer surface. The force-field grid energy (sum of van der Waals and Coulomb energies) was used as the primary scoring function while the Zou GB/SA score (H—Y. Liu et al., J. Phys. Chem. B, (2004), 108, 5453-5462)) was used as the secondary scoring function. The DOCK output .mol2 files for each compound, giving the scores (energies) and the docked poses, were then processed by the program Binding Response (S. Zhong and A. D. MacKerell, J. Chem. Inf. Model., (2007), 47, 2302-2315) to obtain n, the number of docked molecule atoms enclosed by the docking site. Sorting the output, a total of 361 compounds were chosen for the second stage of virtual screening on the basis of the highest grid score, GB/SA score, and n.

The second stage of virtual screening was done with the program Surflex-Dock v.2.3 (A. N. Jain, J. Comput.-Aided Mol. Design, (2007), 21, 281-306), within Sybyl v.8.1 (Tripos Inc., St. Louis, USA). In docking with this program, the GeomX docking option was used with the number of additional starting conformations per molecule increased to 10 and the soft grid treatment turned off. From the docked poses, the top scoring molecules (Total score greater than 4.0, ‘Crash’ component of the score greater than −1.0) were visually examined and 6 compounds available from ChemBridge Corp. (San Diego, USA) were selected for purchase. These compounds are set out in Table 5.

TABLE 5 Compound ID Molecular Name Molecular Weight 7996209 N-[2-(4-methylphenyl)-2-oxoethyl]- 323.3 1-oxo-3,4-dihydro-1H-isochromene- 3-carboxamide 7780327 2-methyl-3-{[(3- 299.2 methylphenoxy)acetyl]amino}benzoic acid 7302096 3-{[(2,5- 319.3 dimethoxyphenyl)amino]carbonyl}-7- oxabicyclo[2.2.1]hept-5-ene-2- carboxylic acid 5785027 2-{2-[(2-hydroxyethyl)amino]-1H- 426.3 benzimidazol-1-yl}-1-(1- naphthyl)ethanone hydrobromide 9124833 3-methoxy-4-[2-(4-morpholinyl)-2- 266.3 oxoethoxy]aniline 7949851 methyl [3-(phenoxyacetyl)-1H-indol- 323.3 1-yl]acetate

Illustrations of these compounds binding to Ab-IgNAR structure are shown in FIGS. 6 to 11.

These 6 compounds were purchased and tested for binding to the Aβ-IgNAR-G1 dimer and IgNAR alone by BIAcore biosensor. No binding definitively above background was observed, perhaps due to the interface targeted ie dimer immobilized, but the cavity targeted was formed by the dimer-tetramer interface.

By way of comparison, docking performed for the anti-inflammatory drug fenofibrate which has been shown to bind Aβ (Kukar et al. Nature 453, 925-929 (2008)

Substrate-targeting-secretase modulators). Docking experiments performed using the structure and a possible modelled solution presented in FIG. 12. No biochemical data for fenofibrate as soaking into crystals cracked the protein crystals, and the insolubility of fenofibrate precluded definitive biosensor experimentation.

It will be appreciated by persons skilled in the art that numerous variations and/or modifications may be made to the invention as shown in the specific embodiments without departing from the spirit or scope of the invention as broadly described. The present embodiments are, therefore, to be considered in all respects as illustrative and not restrictive.

REFERENCES

-   Barghorn, S., V. Nimmrich, et al. (2005). “Globular amyloid     b-peptide oligomer—a homogenous and stable neuropathological protein     in Alzheimer's disease.” J. Neurochem. 95(3): 834-847. -   Bush, A. I. (2000). “Metals and neuroscience.” Curr Opin Chem Biol     4(2): 184-191. -   Crouch, P. J., S.-M. E. Harding, et al. (2008). “Mechanisms of Ab     mediated neurodegeneration in Alzheimer's disease.” Int J Biochem     Cell Biol 40(2): 181-198. -   Culmsee, C. and S. Landshamer (2006). “Molecular insights into     mechanisms of the cell death program: role in the progression of     neurodegenerative disorders.” Curr Alzheimer Res 3(4): 269-83. -   Henderson, K. A., V. A. Streltsov, et al. (2007). “Structure of an     IgNAR-AMA1 complex: targeting a conserved hydrophobic cleft broadens     malarial strain recognition.” Structure 15(11): 1452-66. -   Jang, H., J. Zheng, et al. (2008). “New structures help the modeling     of toxic amyloidbeta ion channels.” Trends Biochem Sci 33(2):     91-100. -   Kajava, A. V., J. M. Squire, et al. (2006). “b-structures in fibrous     proteins.” Adv Protein Chem 73: 1-15. -   Lawrence, M. C. and P. M. Colman (1993). “Shape complementarity at     protein/protein interfaces.” J Mol Biol 234(4): 946-950. -   Losic, D., L. L. Martin, et al. (2006). “High resolution scanning     tunnelling microscopy of the b-amyloid protein (Ab1-40) of     Alzheimer's disease suggests a novel mechanism of oligomer     assembly.” Journal of Structural Biology 155(1): 104-110. -   Luhrs, T., C. Ritter, et al. (2005). “3D structure of Alzheimer's     amyloid-b(1-42) fibrils.” Proc Natl Acad Sci USA 102(48):     17342-17347. -   Malinchik, S. B., H. Inouye, et al. (1998). “Structural analysis of     Alzheimer's b(1-40) amyloid: protofilament assembly of tubular     fibrils.” Biophys. J. 74(1): 537-745. -   Nelson, R. and D. Eisenberg (2006). “Recent atomic models of amyloid     fibril structure.” Curr Opin Struct Biol 16(2): 260-265. -   Nelson, R. and D. Eisenberg (2006). “Structural models of     amyloid-like fibrils.” Adv Protein Chem 73: 235-282. -   Nuttall, S. D., K. S. Humberstone, et al. (2004). “Selection and     affinity maturation of IgNAR variable domains targeting Plasmodium     falciparum AMA1.” Proteins 55(1): 187-97. -   Otwinowski, Z. and W. Minor (1997). “Processing of X-ray Diffraction     Data Collected in Oscillation Mode.” Methods in Enzymology: 307-326. -   Petkova, A. T., Y. Ishii, et al. (2002). “A structural model for     Alzheimer's b-amyloid fibrils based on experimental constraints from     solid state NMR.” Proc Natl Acad Sci USA 99(26): 16742-16747. -   Petkova, A. T., W. M. Yau, et al. (2006). “Experimental constraints     on quaternary structure in Alzheimer's b-amyloid fibrils.”     Biochemistry 4′5(2): 498-512. -   Rahimi, F., A. Shanmugam, et al. (2008). “Structure-function     relationships of pre-fibrillar protein assemblies in Alzheimer's     disease and related disorders.” Curr Alzheimer Res 5(3): 319-41. -   Sato, T., P. Kienlen-Campard, et al. (2006). “Inhibitors of amyloid     toxicity based on b-sheet packing of Ab40 and Ab42.” Biochemistry     45(17): 5503-5516. -   Shankar, G. M., S. Li, et al. (2008). “Amyloid-beta protein dimers     isolated directly from Alzheimer's brains impair synaptic plasticity     and memory.” Nat. Med. -   Streltsov, V. (2008). “X-ray absorption and diffraction studies of     the metal binding sites in amyloid b-peptide.” Eur Biophvs J 37(3):     257-263. -   Streltsov, V. A., J. N. Varghese, et al. (2004). “Structural     evidence for evolution of shark Ig new antigen receptor variable     domain antibodies from a cell-surface receptor.” Proc Natl Acad Sci     USA 101(34): 12444-12449. -   Takano, K., S. Endo, et al. (2006). “Structure of amyloid-b     fragments in aqueous environments.” Febs J 273(1): 150-158. -   Vagin, A. and A. Teplyakov (1997). “MOLREP: an automated program for     molecular replacement.” J. Appl. Crystallogr. 30: 1022-1025. -   Walsh, D. M. (2005). “Disease-associated intra-Ab mutations.”     Alzheimer Research Forum: Available at: http://www.alzgene.org. -   Walsh, D. M. and D. J. Selkoe (2007). “Ab oligomers—a decade of     discovery.” J. Neurochem. 101(5): 1172-1184. -   Wurth, C., N. K. Guimard, et al. (2002). “Mutations that reduce     aggregation of the Alzheimer's Ab42 peptide: an unbiased search for     the sequence determinants of Ab amyloidogenesis.” J Mol Biol 319(5):     1279-1290.

APPENDIX I HEADER Ab-IgNAR REMARK 3 REMARK 3 REFINEMENT. REMARK 3  PROGRAM: REFMAC 5.3.0040 REMARK 3 REMARK 3   REFINEMENT TARGET: MAXIMUM LIKELIHOOD REMARK 3 REMARK 3  DATA USED IN REFINEMENT. REMARK 3  RESOLUTION RANGE HIGH (ANGSTROMS) :  2.20 REMARK 3  RESOLUTION RANGE LOW (ANGSTROMS) :  68.84 REMARK 3  DATA CUTOFF (SIGMA(F)) :  NONE REMARK 3  COMPLETENESS FOR RANGE (%) :  93.45 REMARK 3  NUMBER OF REFLECTIONS :  26860 REMARK 3 REMARK 3  FIT TO DATA USED IN REFINEMENT. REMARK 3  CROSS-VALIDATION METHOD :  THROUGHOUT REMARK 3  FREE R VALUE TEST SET SELECTION :  RANDOM REMARK 3  R VALUE (WORKING + TEST SET) :  0.16841 REMARK 3  R VALUE (WORKING SET) :  0.16431 REMARK 3  FREE R VALUE :  0.24650 REMARK 3  FREE R VALUE TEST SET SIZE (%) :  5.1 REMARK 3  FREE R VALUE TEST SET COUNT :  1439 REMARK 3 REMARK 3  FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3  TOTAL NUMBER OF BINS USED :   20 REMARK 3  BIN RESOLUTION RANGE HIGH : 2.202 REMARK 3  BIN RESOLUTION RANGE LOW : 2.260 REMARK 3  REFLECTION IN BIN (WORKING SET) :  1219 REMARK 3  BIN COMPLETENESS (WORKING + TEST) (%) : 56.98 REMARK 3  BIN R VALUE (WORKING SET) : 0.229 REMARK 3  BIN FREE R VALUE SET COUNT :   55 REMARK 3  BIN FREE R VALUE : 0.307 REMARK 3 REMARK 3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3  ALL ATOMS :   4173 REMARK 3 REMARK 3  B VALUES. REMARK 3  FROM WILSON PLOT (A**2): NULL REMARK 3  MEAN B VALUE    (OVERALL, A**2): 46.544 REMARK 3  OVERALL ANISOTROPIC B VALUE. REMARK 3   B11 (A**2) : 0.05 REMARK 3   B22 (A**2) : 0.05 REMARK 3   B33 (A**2) : −0.08 REMARK 3   B12 (A**2) : 0.03 REMARK 3   B13 (A**2) : 0.00 REMARK 3   B23 (A**2) : 0.00 REMARK 3 REMARK 3  ESTIMATED OVERALL COORDINATE ERROR. REMARK 3  ESU BASED ON R VALUE (A) :   0.241 REMARK 3  ESU BASED ON FREE R VALUE (A) :   0.223 REMARK 3  ESU BASED ON MAXIMUM LIKELIHOOD (A) :   0.152 REMARK 3  ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2):  11.557 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3  CORRELATION COEFFICIENT FO-FC :   0.968 REMARK 3  CORRELATION COEFFICIENT FO-FC FREE :   0.930 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3  BOND LENGTHS REFINED ATOMS (A): 3835 ; 0.022 ; 0.022 REMARK 3  BOND ANGLES REFINED ATOMS (DEGREES): 5173 ; 1.994 ; 1.953 REMARK 3  TORSION ANGLES, PERIOD 1 (DEGREES):  499 ; 7.067 ; 5.000 REMARK 3  TORSION ANGLES, PERIOD 2 (DEGREES):  152 ; 35.901 ;  23.947  REMARK 3  TORSION ANGLES, PERIOD 3 (DEGREES):  664 ; 21.119 ;  15.000  REMARK 3  TORSION ANGLES, PERIOD 4 (DEGREES):  24 ; 14.991 ;  15.000  REMARK 3  CHIRAL-CENTER RESTRAINTS (A**3):  591 ; 0.179 ; 0.200 REMARK 3  GENERAL PLANES REFINED ATOMS (A): 2832 ; 0.008 ; 0.020 REMARK 3  NON-BONDED CONTACTS REFINED ATOMS (A): 1537 ; 0.228 ; 0.200 REMARK 3  NON-BONDED TORSION REFINED ATOMS (A): 2516 ; 0.311 ; 0.200 REMARK 3  H-BOND (X...Y) REFINED ATOMS (A):  292 ; 0.240 ; 0.200 REMARK 3  SYMMETRY VDW REFINED ATOMS (A):  52 ; 0.222 ; 0.200 REMARK 3  SYMMETRY H-BOND REFINED ATOMS (A):  22 ; 0.298 ; 0.200 REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3  MAIN-CHAIN BOND REFINED ATOMS (A**2): 2501 ; 1.051 ; 1.500 REMARK 3  MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3921 ; 1.795 ; 2.000 REMARK 3  SIDE-CHAIN BOND REFINED ATOMS (A**2): 1515 ; 3.032 ; 3.000 REMARK 3  SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1252 ; 4.656 ; 4.500 REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS :   4 REMARK 3 ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY REMARK 3 REMARK 3 TLS GROUP :   1 REMARK 3 NUMBER OF COMPONENTS GROUP :   1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE: A 1 A 126 REMARK 3 ORIGIN FOR THE GROUP (A): 63.8110 0.9650 −21.6740 REMARK 3 T TENSOR REMARK 3  T11: −0.1980 T22: −0.2050 REMARK 3  T33: −0.1620 T12: 0.0369 REMARK 3  T13: 0.0437 T23: 0.0680 REMARK 3 L TENSOR REMARK 3  L11: 2.9649 L22: 2.1492 REMARK 3  L33: 5.5016 L12: 1.6240 REMARK 3  L13: −3.1186 L23: −1.7013 REMARK 3 S TENSOR REMARK 3  S11: −0.1563 S12: 0.1452 S13: −0.2168 REMARK 3  S21: −0.3866 S22: 0.0489 S23: −0.3471 REMARK 3  S31: 0.2723 S32: −0.1279 S33: 0.1075 REMARK 3 REMARK 3 TLS GROUP :   2 REMARK 3 NUMBER OF COMPONENTS GROUP :   1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE: B 1 B 126 REMARK 3 ORIGIN FOR THE GROUP (A): 22.5770 −14.1900 −12.2800 REMARK 3 T TENSOR REMARK 3  T11: −0.0751 T22: −0.1155 REMARK 3  T33: −0.1816 T12: −0.0421 REMARK 3  T13: −0.0399 T23: −0.0558 REMARK 3 L TENSOR REMARK 3  L11: 10.1470 L22: 1.3573 REMARK 3  L33: 3.5880 L12: 1.6659 REMARK 3  L13: 3.8599 L23: 0.8640 REMARK 3 S TENSOR REMARK 3  S11: 0.2336 S12: −0.7625 S13: −0.3980 REMARK 3  S21: 0.2329 S22: −0.2032 S23: −0.1926 REMARK 3  S31: 0.0115 S32: −0.2069 S33: −0.0305 REMARK 3 REMARK 3 TLS GROUP :   3 REMARK 3 NUMBER OF COMPONENTS GROUP :   1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE: C 1 C 126 REMARK 3 ORIGIN FOR THE GROUP (A): 35.8140 7.3450 5.8670 REMARK 3 T TENSOR REMARK 3  T11: −0.1853 T22: −0.1041 REMARK 3  T33: −0.2449 T12: 0.0111 REMARK 3  T13: −0.0203 T23: −0.0062 REMARK 3 L TENSOR REMARK 3  L11: 2.6982 L22: 1.5248 REMARK 3  L33: 3.8494 L12: −1.7131 REMARK 3  L13: −3.2164 L23: 2.1240 REMARK 3 S TENSOR REMARK 3  S11: −0.1201 S12: −0.0335 S13: 0.0035 REMARK 3  S21: 0.0881 S22: −0.0407 S23: 0.0913 REMARK 3  S31: 0.1124 S32: 0.0662 S33: 0.1608 REMARK 3 REMARK 3 TLS GROUP :   4 REMARK 3 NUMBER OF COMPONENTS GROUP :   1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE: D 1 D 125 REMARK 3 ORIGIN FOR THE GROUP (A): 59.5290 −29.2800 −4.2380 REMARK 3 T TENSOR REMARK 3  T11: 0.0220 T22: −0.0010 REMARK 3  T33: −0.1489 T12: 0.0046 REMARK 3  T13: 0.0795 T23: 0.0694 REMARK 3 L TENSOR REMARK 3  L11: 2.7989 L22: 9.7864 REMARK 3  L33: 4.7502 L12: −4.5612 REMARK 3  L13: 2.9365 L23: −5.7275 REMARK 3 S TENSOR REMARK 3  S11: 0.4188 S12: 0.4905 S13: 0.0482 REMARK 3  S21: −0.7846 S22: −0.4194 S23: 0.2228 REMARK 3  S31: 0.4959 S32: 0.5328 S33: 0.0006 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3  METHOD USED : MASK REMARK 3  PARAMETERS FOR MASK CALCULATION REMARK 3  VDW PROBE RADIUS : 1.20 REMARK 3  ION PROBE RADIUS : 0.80 REMARK 3  SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3  OTHER REFINEMENT REMARKS: REMARK 3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS REMARK 3 SSBOND 1 CYS A 22 CYS A 83 SSBOND 2 CYS B 22 CYS B 83 SSBOND 3 CYS C 22 CYS C 83 SSBOND 4 CYS D 22 CYS D 83 CISPEP 1 THR A  6 PRO A  7 0.00 CISPEP 2 THR D  6 PRO D  7 0.00 CISPEP 3 THR B  6 PRO B  7 0.00 CISPEP 4 THR C  6 PRO C  7 0.00 CRYST1 79.399 79.399 84.890 90.00 90.00 120.00 P 32 SCALE1 0.012595  0.007272  0.000000 0.00000 SCALE2 0.000000  0.014543  0.000000 0.00000 SCALE3 0.000000  0.000000  0.011780 0.00000 ATOM 1 N ALA A 1 61.749 8.643 −7.895 1.00 40.15 N ATOM 2 CA ALA A 1 62.634 7.902 −8.884 1.00 40.18 C ATOM 3 CB ALA A 1 62.339 6.518 −8.853 1.00 39.79 C ATOM 4 C ALA A 1 62.285 8.403 −10.269 1.00 40.24 C ATOM 5 O ALA A 1 61.183 8.874 −10.490 1.00 40.36 O ATOM 6 N TRP A 2 63.195 8.273 −11.213 1.00 39.60 N ATOM 7 CA TRP A 2 62.842 8.487 −12.631 1.00 39.57 C ATOM 8 CB TRP A 2 62.870 9.972 −12.978 1.00 38.16 C ATOM 9 CG TRP A 2 64.196 10.736 −12.660 1.00 37.18 C ATOM 10 CD1 TRP A 2 64.695 11.043 −11.419 1.00 36.93 C ATOM 11 NE1 TRP A 2 65.878 11.763 −11.534 1.00 39.31 N ATOM 12 CE2 TRP A 2 66.153 11.943 −12.869 1.00 37.67 C ATOM 13 CD2 TRP A 2 65.132 11.298 −13.609 1.00 36.59 C ATOM 14 CE3 TRP A 2 65.173 11.364 −15.011 1.00 37.43 C ATOM 15 CZ3 TRP A 2 66.223 12.030 −15.622 1.00 37.01 C ATOM 16 CH2 TRP A 2 67.259 12.614 −14.864 1.00 37.70 C ATOM 17 CZ2 TRP A 2 67.247 12.571 −13.485 1.00 38.75 C ATOM 18 C TRP A 2 63.930 7.731 −13.337 1.00 40.62 C ATOM 19 O TRP A 2 64.970 7.444 −12.740 1.00 41.17 O ATOM 20 N VAL A 3 63.713 7.420 −14.598 1.00 41.79 N ATOM 21 CA VAL A 3 64.712 6.737 −15.393 1.00 41.23 C ATOM 22 CB VAL A 3 64.067 5.575 −16.107 1.00 42.49 C ATOM 23 CG1 VAL A 3 65.010 5.042 −17.208 1.00 41.14 C ATOM 24 CG2 VAL A 3 63.708 4.417 −15.072 1.00 42.49 C ATOM 25 C VAL A 3 65.240 7.752 −16.400 1.00 42.26 C ATOM 26 O VAL A 3 64.461 8.371 −17.135 1.00 39.69 O ATOM 27 N ASP A 4 66.560 7.946 −16.388 1.00 42.27 N ATOM 28 CA ASP A 4 67.259 8.833 −17.277 1.00 42.47 C ATOM 29 CB ASP A 4 68.484 9.335 −16.509 1.00 44.28 C ATOM 30 CG ASP A 4 69.123 10.573 −17.112 1.00 43.29 C ATOM 31 OD1 ASP A 4 68.608 11.128 −18.127 1.00 41.54 O ATOM 32 OD2 ASP A 4 70.150 10.991 −16.507 1.00 47.28 O ATOM 33 C ASP A 4 67.725 8.103 −18.544 1.00 42.79 C ATOM 34 O ASP A 4 68.709 7.350 −18.523 1.00 43.97 O ATOM 35 N GLN A 5 67.048 8.361 −19.639 1.00 42.16 N ATOM 36 CA GLN A 5 67.299 7.703 −20.903 1.00 43.25 C ATOM 37 CB GLN A 5 65.983 7.258 −21.571 1.00 42.36 C ATOM 38 CG GLN A 5 66.230 6.429 −22.844 1.00 43.49 C ATOM 39 CD GLN A 5 64.959 5.836 −23.412 1.00 43.79 C ATOM 40 OE1 GLN A 5 63.975 5.772 −22.714 1.00 45.41 O ATOM 41 NE2 GLN A 5 64.976 5.402 −24.693 1.00 41.11 N ATOM 42 C GLN A 5 68.052 8.629 −21.864 1.00 42.68 C ATOM 43 O GLN A 5 67.584 9.724 −22.191 1.00 41.82 O ATOM 44 N THR A 6 69.198 8.157 −22.354 1.00 42.97 N ATOM 45 CA THR A 6 69.971 8.908 −23.364 1.00 42.86 C ATOM 46 CB THR A 6 71.203 9.619 −22.713 1.00 43.54 C ATOM 47 OG1 THR A 6 71.985 8.617 −22.080 1.00 44.91 O ATOM 48 CG2 THR A 6 70.801 10.670 −21.649 1.00 41.18 C ATOM 49 C THR A 6 70.442 8.007 −24.507 1.00 43.00 C ATOM 50 O THR A 6 70.734 6.818 −24.262 1.00 44.11 O ATOM 51 N PRO A 7 70.571 8.561 −25.757 1.00 42.63 N ATOM 52 CA PRO A 7 70.323 9.961 −26.145 1.00 42.77 C ATOM 53 CB PRO A 7 71.057 10.081 −27.477 1.00 41.46 C ATOM 54 CG PRO A 7 70.903 8.752 −28.078 1.00 41.46 C ATOM 55 CD PRO A 7 71.052 7.779 −26.918 1.00 43.08 C ATOM 56 C PRO A 7 68.835 10.178 −26.359 1.00 43.23 C ATOM 57 O PRO A 7 68.177 9.198 −26.651 1.00 44.91 O ATOM 58 N ARG A 8 68.302 11.392 −26.222 1.00 43.41 N ATOM 59 CA ARG A 8 66.868 11.625 −26.493 1.00 44.08 C ATOM 60 CB ARG A 8 66.349 12.944 −25.869 1.00 43.76 C ATOM 61 CG ARG A 8 64.763 13.006 −25.738 1.00 46.28 C ATOM 62 CD ARG A 8 64.248 13.844 −24.561 1.00 48.21 C ATOM 63 NE ARG A 8 64.530 13.270 −23.235 1.00 51.99 N ATOM 64 CZ ARG A 8 64.574 13.982 −22.102 1.00 49.58 C ATOM 65 NH1 ARG A 8 64.388 15.306 −22.123 1.00 45.49 N ATOM 66 NH2 ARG A 8 64.817 13.367 −20.953 1.00 50.31 N ATOM 67 C ARG A 8 66.538 11.587 −27.988 1.00 43.51 C ATOM 68 O ARG A 8 65.418 11.284 −28.370 1.00 43.05 O ATOM 69 N THR A 9 67.498 11.929 −28.846 1.00 42.86 N ATOM 70 CA THR A 9 67.285 11.777 −30.274 1.00 43.57 C ATOM 71 CB THR A 9 66.814 13.095 −30.939 1.00 43.56 C ATOM 72 OG1 THR A 9 67.858 14.036 −30.821 1.00 48.77 O ATOM 73 CG2 THR A 9 65.563 13.731 −30.225 1.00 43.75 C ATOM 74 C THR A 9 68.564 11.279 −30.904 1.00 42.93 C ATOM 75 O THR A 9 69.650 11.556 −30.398 1.00 43.89 O ATOM 76 N ALA A 10 68.453 10.511 −31.978 1.00 42.78 N ATOM 77 CA ALA A 10 69.619 9.970 −32.667 1.00 42.32 C ATOM 78 CB ALA A 10 69.994 8.627 −32.086 1.00 42.83 C ATOM 79 C ALA A 10 69.314 9.859 −34.149 1.00 43.20 C ATOM 80 O ALA A 10 68.155 9.623 −34.518 1.00 43.17 O ATOM 81 N THR A 11 70.318 10.143 −34.992 1.00 42.97 N ATOM 82 CA THR A 11 70.225 9.915 −36.444 1.00 43.50 C ATOM 83 CB THR A 11 70.189 11.203 −37.289 1.00 43.99 C ATOM 84 OG1 THR A 11 69.173 12.071 −36.792 1.00 46.81 O ATOM 85 CG2 THR A 11 69.888 10.919 −38.782 1.00 44.63 C ATOM 86 C THR A 11 71.394 9.035 −36.818 1.00 42.68 C ATOM 87 O THR A 11 72.527 9.265 −36.405 1.00 42.50 O ATOM 88 N LYS A 12 71.095 7.988 −37.565 1.00 42.11 N ATOM 89 CA LYS A 12 72.062 6.984 −37.863 1.00 41.61 C ATOM 90 CB LYS A 12 71.742 5.752 −37.024 1.00 42.20 C ATOM 91 CG LYS A 12 72.682 5.566 −35.832 1.00 42.69 C ATOM 92 CD LYS A 12 72.462 6.488 −34.722 1.00 42.75 C ATOM 93 CE LYS A 12 73.785 6.938 −34.193 1.00 45.64 C ATOM 94 NZ LYS A 12 74.413 5.947 −33.372 1.00 45.06 N ATOM 95 C LYS A 12 72.005 6.639 −39.319 1.00 41.13 C ATOM 96 O LYS A 12 70.939 6.763 −39.917 1.00 40.78 O ATOM 97 N GLU A 13 73.148 6.221 −39.886 1.00 41.13 N ATOM 98 CA GLU A 13 73.217 5.639 −41.224 1.00 41.27 C ATOM 99 CB GLU A 13 74.632 5.698 −41.828 1.00 42.20 C ATOM 100 CG GLU A 13 75.229 7.083 −41.972 1.00 45.88 C ATOM 101 CD GLU A 13 74.375 8.034 −42.822 1.00 46.51 C ATOM 102 OE1 GLU A 13 74.450 9.257 −42.598 1.00 46.46 O ATOM 103 OE2 GLU A 13 73.643 7.546 −43.710 1.00 49.37 O ATOM 104 C GLU A 13 72.800 4.187 −41.192 1.00 40.83 C ATOM 105 O GLU A 13 72.992 3.508 −40.169 1.00 41.54 O ATOM 106 N THR A 14 72.215 3.721 −42.301 1.00 40.03 N ATOM 107 CA THR A 14 71.940 2.318 −42.489 1.00 39.84 C ATOM 108 CB THR A 14 71.377 2.042 −43.909 1.00 40.21 C ATOM 109 OG1 THR A 14 69.983 2.377 −43.955 1.00 37.92 O ATOM 110 CG2 THR A 14 71.526 0.563 −44.299 1.00 39.74 C ATOM 111 C THR A 14 73.270 1.599 −42.243 1.00 40.13 C ATOM 112 O THR A 14 74.324 2.000 −42.791 1.00 39.27 O ATOM 113 N GLY A 15 73.233 0.613 −41.342 1.00 40.34 N ATOM 114 CA GLY A 15 74.396 −0.218 −41.032 1.00 40.42 C ATOM 115 C GLY A 15 75.117 0.128 −39.748 1.00 40.96 C ATOM 116 O GLY A 15 75.788 −0.709 −39.224 1.00 41.04 O ATOM 117 N GLU A 16 74.989 1.365 −39.256 1.00 41.99 N ATOM 118 CA GLU A 16 75.598 1.850 −38.014 1.00 43.51 C ATOM 119 CB GLU A 16 75.343 3.359 −37.860 1.00 43.93 C ATOM 120 CG GLU A 16 76.304 4.377 −38.538 1.00 45.03 C ATOM 121 CD GLU A 16 76.197 5.807 −37.839 1.00 46.94 C ATOM 122 OE1 GLU A 16 75.428 6.678 −38.323 1.00 43.22 O ATOM 123 OE2 GLU A 16 76.837 6.036 −36.754 1.00 52.94 O ATOM 124 C GLU A 16 74.854 1.177 −36.872 1.00 43.56 C ATOM 125 O GLU A 16 73.865 0.509 −37.092 1.00 43.77 O ATOM 126 N SER A 17 75.282 1.388 −35.641 1.00 43.74 N ATOM 127 CA SER A 17 74.492 0.923 −34.544 1.00 44.40 C ATOM 128 CB SER A 17 75.215 −0.229 −33.873 1.00 44.97 C ATOM 129 OG SER A 17 76.123 0.270 −32.945 1.00 50.00 O ATOM 130 C SER A 17 74.111 2.054 −33.578 1.00 44.40 C ATOM 131 O SER A 17 74.564 3.183 −33.740 1.00 43.42 O ATOM 132 N LEU A 18 73.218 1.768 −32.623 1.00 44.29 N ATOM 133 CA LEU A 18 72.750 2.743 −31.631 1.00 43.42 C ATOM 134 CB LEU A 18 71.264 3.018 −31.857 1.00 44.02 C ATOM 135 CG LEU A 18 70.458 4.188 −31.246 1.00 45.03 C ATOM 136 CD1 LEU A 18 69.189 3.777 −30.570 1.00 43.77 C ATOM 137 CD2 LEU A 18 71.201 5.339 −30.494 1.00 43.20 C ATOM 138 C LEU A 18 72.893 2.116 −30.251 1.00 43.15 C ATOM 139 O LEU A 18 72.533 0.967 −30.042 1.00 42.50 O ATOM 140 N THR A 19 73.396 2.881 −29.305 1.00 42.18 N ATOM 141 CA THR A 19 73.367 2.460 −27.919 1.00 42.94 C ATOM 142 CB THR A 19 74.762 2.333 −27.352 1.00 41.91 C ATOM 143 OG1 THR A 19 75.459 1.366 −28.144 1.00 46.16 O ATOM 144 CG2 THR A 19 74.690 1.835 −25.920 1.00 43.14 C ATOM 145 C THR A 19 72.566 3.445 −27.107 1.00 42.46 C ATOM 146 O THR A 19 72.838 4.656 −27.120 1.00 42.53 O ATOM 147 N ILE A 20 71.548 2.927 −26.451 1.00 42.31 N ATOM 148 CA ILE A 20 70.689 3.706 −25.552 1.00 43.03 C ATOM 149 CB ILE A 20 69.201 3.335 −25.767 1.00 43.33 C ATOM 150 CG1 ILE A 20 68.800 3.502 −27.256 1.00 44.11 C ATOM 151 CD1 ILE A 20 67.399 2.948 −27.600 1.00 44.88 C ATOM 152 CG2 ILE A 20 68.302 4.141 −24.822 1.00 42.84 C ATOM 153 C ILE A 20 71.077 3.333 −24.134 1.00 42.61 C ATOM 154 O ILE A 20 71.157 2.147 −23.843 1.00 41.82 O ATOM 155 N ASN A 21 71.379 4.327 −23.294 1.00 43.17 N ATOM 156 CA ASN A 21 71.708 4.102 −21.860 1.00 44.83 C ATOM 157 CB ASN A 21 72.990 4.831 −21.455 1.00 44.74 C ATOM 158 CG ASN A 21 74.197 4.409 −22.296 1.00 50.81 C ATOM 159 OD1 ASN A 21 74.786 3.335 −22.070 1.00 57.38 O ATOM 160 ND2 ASN A 21 74.594 5.257 −23.256 1.00 52.86 N ATOM 161 C ASN A 21 70.569 4.588 −20.961 1.00 45.00 C ATOM 162 O ASN A 21 70.033 5.670 −21.182 1.00 44.50 O ATOM 163 N CYS A 22 70.208 3.816 −19.949 1.00 44.60 N ATOM 164 CA CYS A 22 69.167 4.237 −19.029 1.00 45.32 C ATOM 165 CB CYS A 22 67.909 3.372 −19.165 1.00 45.74 C ATOM 166 SG CYS A 22 66.995 3.746 −20.639 1.00 54.23 S ATOM 167 C CYS A 22 69.658 4.101 −17.624 1.00 44.15 C ATOM 168 O CYS A 22 70.236 3.107 −17.289 1.00 43.54 O ATOM 169 N VAL A 23 69.395 5.085 −16.785 1.00 43.49 N ATOM 170 CA VAL A 23 69.643 4.909 −15.365 1.00 42.35 C ATOM 171 CB VAL A 23 71.085 5.352 −14.883 1.00 43.00 C ATOM 172 CG1 VAL A 23 71.963 6.041 −15.953 1.00 41.73 C ATOM 173 CG2 VAL A 23 71.199 5.917 −13.413 1.00 42.45 C ATOM 174 C VAL A 23 68.417 5.249 −14.481 1.00 42.71 C ATOM 175 O VAL A 23 67.709 6.260 −14.671 1.00 41.74 O ATOM 176 N LEU A 24 68.123 4.344 −13.563 1.00 42.36 N ATOM 177 CA LEU A 24 67.057 4.563 −12.645 1.00 43.14 C ATOM 178 CB LEU A 24 66.608 3.213 −12.068 1.00 43.10 C ATOM 179 CG LEU A 24 65.662 3.260 −10.863 1.00 44.67 C ATOM 180 CD1 LEU A 24 64.281 3.811 −11.337 1.00 42.56 C ATOM 181 CD2 LEU A 24 65.508 1.885 −10.150 1.00 44.14 C ATOM 182 C LEU A 24 67.691 5.476 −11.592 1.00 42.20 C ATOM 183 O LEU A 24 68.575 5.053 −10.877 1.00 42.62 O ATOM 184 N ARG A 25 67.261 6.734 −11.531 1.00 41.75 N ATOM 185 CA ARG A 25 67.859 7.731 −10.598 1.00 40.94 C ATOM 186 CB ARG A 25 68.196 9.032 −11.327 1.00 39.67 C ATOM 187 CG ARG A 25 69.067 8.832 −12.554 1.00 39.63 C ATOM 188 CD ARG A 25 69.891 10.080 −12.859 1.00 38.88 C ATOM 189 NE ARG A 25 70.828 9.833 −13.950 1.00 44.89 N ATOM 190 CZ ARG A 25 72.121 9.535 −13.783 1.00 47.29 C ATOM 191 NH1 ARG A 25 72.620 9.447 −12.539 1.00 46.01 N ATOM 192 NH2 ARG A 25 72.924 9.391 −14.850 1.00 43.92 N ATOM 193 C ARG A 25 66.903 8.056 −9.468 1.00 41.31 C ATOM 194 O ARG A 25 65.691 7.828 −9.600 1.00 39.67 O ATOM 195 N ASP A 26 67.466 8.586 −8.375 1.00 41.32 N ATOM 196 CA ASP A 26 66.756 8.989 −7.190 1.00 43.62 C ATOM 197 CB ASP A 26 66.179 10.401 −7.349 1.00 45.00 C ATOM 198 CG ASP A 26 67.224 11.395 −7.953 1.00 52.91 C ATOM 199 OD1 ASP A 26 66.854 12.215 −8.853 1.00 59.13 O ATOM 200 OD2 ASP A 26 68.436 11.347 −7.556 1.00 60.06 O ATOM 201 C ASP A 26 65.732 7.986 −6.674 1.00 43.23 C ATOM 202 O ASP A 26 64.635 8.350 −6.232 1.00 43.09 O ATOM 203 N ALA A 27 66.114 6.708 −6.710 1.00 43.21 N ATOM 204 CA ALA A 27 65.231 5.600 −6.311 1.00 42.66 C ATOM 205 CB ALA A 27 65.081 4.609 −7.466 1.00 40.95 C ATOM 206 C ALA A 27 65.800 4.898 −5.058 1.00 43.66 C ATOM 207 O ALA A 27 66.997 4.563 −4.986 1.00 43.64 O ATOM 208 N SER A 28 64.929 4.643 −4.097 1.00 44.63 N ATOM 209 CA SER A 28 65.301 3.945 −2.860 1.00 46.25 C ATOM 210 CB SER A 28 64.306 4.340 −1.793 1.00 46.62 C ATOM 211 OG SER A 28 62.989 4.076 −2.343 1.00 51.66 O ATOM 212 C SER A 28 65.244 2.424 −3.024 1.00 45.27 C ATOM 213 O SER A 28 65.753 1.699 −2.204 1.00 45.50 O ATOM 214 N PHE A 29 64.597 1.951 −4.080 1.00 44.65 N ATOM 215 CA PHE A 29 64.428 0.515 −4.320 1.00 44.66 C ATOM 216 CB PHE A 29 63.026 0.206 −4.853 1.00 44.20 C ATOM 217 CG PHE A 29 62.491 1.236 −5.821 1.00 43.80 C ATOM 218 CD1 PHE A 29 61.557 2.181 −5.392 1.00 42.75 C ATOM 219 CE1 PHE A 29 61.055 3.155 −6.275 1.00 42.50 C ATOM 220 CZ PHE A 29 61.457 3.156 −7.641 1.00 42.43 C ATOM 221 CE2 PHE A 29 62.376 2.202 −8.074 1.00 43.56 C ATOM 222 CD2 PHE A 29 62.895 1.243 −7.168 1.00 40.83 C ATOM 223 C PHE A 29 65.444 0.022 −5.324 1.00 44.85 C ATOM 224 O PHE A 29 66.046 0.816 −6.017 1.00 45.13 O ATOM 225 N GLU A 30 65.606 −1.292 −5.428 1.00 44.65 N ATOM 226 CA GLU A 30 66.616 −1.829 −6.302 1.00 45.34 C ATOM 227 CB GLU A 30 67.141 −3.148 −5.719 1.00 46.03 C ATOM 228 CG GLU A 30 67.484 −3.139 −4.182 1.00 51.87 C ATOM 229 CD GLU A 30 68.905 −2.718 −3.833 1.00 61.36 C ATOM 230 OE1 GLU A 30 69.655 −3.533 −3.218 1.00 64.71 O ATOM 231 OE2 GLU A 30 69.283 −1.554 −4.132 1.00 66.90 O ATOM 232 C GLU A 30 66.040 −2.045 −7.710 1.00 44.87 C ATOM 233 O GLU A 30 64.804 −2.206 −7.902 1.00 43.77 O ATOM 234 N LEU A 31 66.933 −2.100 −8.692 1.00 44.05 N ATOM 235 CA LEU A 31 66.527 −2.480 −10.022 1.00 44.47 C ATOM 236 CB LEU A 31 67.529 −1.966 −11.057 1.00 44.35 C ATOM 237 CG LEU A 31 67.302 −2.279 −12.541 1.00 44.08 C ATOM 238 CD1 LEU A 31 68.569 −2.051 −13.351 1.00 41.58 C ATOM 239 CD2 LEU A 31 66.136 −1.523 −13.132 1.00 41.76 C ATOM 240 C LEU A 31 66.373 −4.001 −10.047 1.00 45.45 C ATOM 241 O LEU A 31 67.337 −4.736 −9.819 1.00 46.74 O ATOM 242 N LYS A 32 65.139 −4.478 −10.238 1.00 45.05 N ATOM 243 CA LYS A 32 64.876 −5.919 −10.271 1.00 44.49 C ATOM 244 CB LYS A 32 63.509 −6.221 −9.649 1.00 44.92 C ATOM 245 CG LYS A 32 63.393 −5.867 −8.121 1.00 46.76 C ATOM 246 CD LYS A 32 64.441 −6.598 −7.239 1.00 46.19 C ATOM 247 CE LYS A 32 63.953 −6.546 −5.816 1.00 50.58 C ATOM 248 NZ LYS A 32 64.928 −7.103 −4.883 1.00 53.68 N ATOM 249 C LYS A 32 64.934 −6.509 −11.676 1.00 44.11 C ATOM 250 O LYS A 32 65.328 −7.643 −11.858 1.00 42.45 O ATOM 251 N ASP A 33 64.509 −5.743 −12.676 1.00 44.84 N ATOM 252 CA ASP A 33 64.436 −6.261 −14.076 1.00 44.80 C ATOM 253 CB ASP A 33 63.261 −7.211 −14.233 1.00 45.40 C ATOM 254 CG ASP A 33 63.419 −8.179 −15.400 1.00 49.24 C ATOM 255 OD1 ASP A 33 64.455 −8.192 −16.141 1.00 47.77 O ATOM 256 OD2 ASP A 33 62.433 −8.933 −15.577 1.00 55.63 O ATOM 257 C ASP A 33 64.293 −5.127 −15.063 1.00 44.19 C ATOM 258 O ASP A 33 64.063 −3.981 −14.671 1.00 42.88 O ATOM 259 N THR A 34 64.481 −5.431 −16.348 1.00 43.32 N ATOM 260 CA THR A 34 64.513 −4.362 −17.365 1.00 42.96 C ATOM 261 CB THR A 34 65.977 −4.082 −17.816 1.00 43.35 C ATOM 262 OG1 THR A 34 66.616 −5.313 −18.245 1.00 46.20 O ATOM 263 CG2 THR A 34 66.799 −3.582 −16.631 1.00 42.87 C ATOM 264 C THR A 34 63.634 −4.801 −18.566 1.00 42.17 C ATOM 265 O THR A 34 63.395 −6.018 −18.771 1.00 40.33 O ATOM 266 N GLY A 35 63.143 −3.820 −19.318 1.00 40.76 N ATOM 267 CA GLY A 35 62.446 −4.100 −20.554 1.00 40.48 C ATOM 268 C GLY A 35 62.659 −2.980 −21.531 1.00 40.71 C ATOM 269 O GLY A 35 63.001 −1.868 −21.139 1.00 41.72 O ATOM 270 N TRP A 36 62.465 −3.294 −22.815 1.00 40.28 N ATOM 271 CA TRP A 36 62.674 −2.399 −23.935 1.00 40.14 C ATOM 272 CB TRP A 36 63.993 −2.767 −24.656 1.00 38.78 C ATOM 273 CG TRP A 36 65.201 −2.495 −23.763 1.00 37.14 C ATOM 274 CD1 TRP A 36 65.778 −3.349 −22.867 1.00 36.99 C ATOM 275 NE1 TRP A 36 66.846 −2.715 −22.216 1.00 37.64 N ATOM 276 CE2 TRP A 36 66.915 −1.410 −22.659 1.00 37.73 C ATOM 277 CD2 TRP A 36 65.912 −1.233 −23.632 1.00 35.75 C ATOM 278 CE3 TRP A 36 65.771 0.021 −24.231 1.00 38.30 C ATOM 279 CZ3 TRP A 36 66.662 1.028 −23.895 1.00 38.55 C ATOM 280 CH2 TRP A 36 67.669 0.808 −22.922 1.00 38.11 C ATOM 281 CZ2 TRP A 36 67.803 −0.388 −22.308 1.00 39.69 C ATOM 282 C TRP A 36 61.462 −2.494 −24.882 1.00 40.45 C ATOM 283 O TRP A 36 60.900 −3.575 −25.086 1.00 37.84 O ATOM 284 N TYR A 37 61.082 −1.350 −25.466 1.00 40.70 N ATOM 285 CA TYR A 37 59.866 −1.236 −26.308 1.00 41.93 C ATOM 286 CB TYR A 37 58.685 −0.707 −25.468 1.00 42.76 C ATOM 287 CG TYR A 37 58.563 −1.427 −24.194 1.00 42.14 C ATOM 288 CD1 TYR A 37 57.719 −2.520 −24.075 1.00 40.34 C ATOM 289 CE1 TYR A 37 57.646 −3.242 −22.868 1.00 41.85 C ATOM 290 CZ TYR A 37 58.426 −2.826 −21.801 1.00 42.69 C ATOM 291 OH TYR A 37 58.379 −3.479 −20.599 1.00 47.21 O ATOM 292 CE2 TYR A 37 59.238 −1.728 −21.895 1.00 42.12 C ATOM 293 CD2 TYR A 37 59.307 −1.027 −23.098 1.00 41.52 C ATOM 294 C TYR A 37 60.081 −0.257 −27.427 1.00 42.18 C ATOM 295 O TYR A 37 60.936 0.595 −27.346 1.00 41.61 O ATOM 296 N ARG A 38 59.267 −0.357 −28.453 1.00 43.78 N ATOM 297 CA ARG A 38 59.532 0.406 −29.648 1.00 46.16 C ATOM 298 CB ARG A 38 60.599 −0.320 −30.467 1.00 45.76 C ATOM 299 CG ARG A 38 60.521 −0.353 −31.940 1.00 49.53 C ATOM 300 CD ARG A 38 61.333 −1.543 −32.436 1.00 50.13 C ATOM 301 NE ARG A 38 60.989 −1.847 −33.794 1.00 52.73 N ATOM 302 CZ ARG A 38 61.856 −1.891 −34.805 1.00 60.11 C ATOM 303 NH1 ARG A 38 61.402 −2.162 −36.023 1.00 59.27 N ATOM 304 NH2 ARG A 38 63.172 −1.662 −34.620 1.00 60.83 N ATOM 305 C ARG A 38 58.216 0.686 −30.345 1.00 46.60 C ATOM 306 O ARG A 38 57.320 −0.172 −30.373 1.00 46.42 O ATOM 307 N THR A 39 58.077 1.929 −30.802 1.00 46.84 N ATOM 308 CA THR A 39 56.980 2.339 −31.664 1.00 47.57 C ATOM 309 CB THR A 39 56.261 3.586 −31.110 1.00 47.10 C ATOM 310 OG1 THR A 39 55.916 3.378 −29.750 1.00 50.61 O ATOM 311 CG2 THR A 39 54.999 3.839 −31.858 1.00 49.14 C ATOM 312 C THR A 39 57.637 2.703 −32.961 1.00 47.84 C ATOM 313 O THR A 39 58.482 3.618 −32.983 1.00 46.61 O ATOM 314 N LYS A 40 57.283 1.980 −34.034 1.00 49.00 N ATOM 315 CA LYS A 40 57.849 2.253 −35.349 1.00 51.32 C ATOM 316 CB LYS A 40 57.656 1.095 −36.329 1.00 51.60 C ATOM 317 CG LYS A 40 58.368 −0.180 −35.877 1.00 54.32 C ATOM 318 CD LYS A 40 58.208 −1.327 −36.858 1.00 55.56 C ATOM 319 CE LYS A 40 59.149 −1.119 −38.039 1.00 55.54 C ATOM 320 NZ LYS A 40 59.491 −2.440 −38.640 1.00 58.58 N ATOM 321 C LYS A 40 57.310 3.555 −35.909 1.00 51.81 C ATOM 322 O LYS A 40 56.245 4.013 −35.513 1.00 51.60 O ATOM 323 N LEU A 41 58.073 4.166 −36.805 1.00 53.16 N ATOM 324 CA LEU A 41 57.623 5.383 −37.454 1.00 54.73 C ATOM 325 CB LEU A 41 58.735 5.951 −38.319 1.00 55.27 C ATOM 326 CG LEU A 41 58.569 7.373 −38.833 1.00 56.10 C ATOM 327 CD1 LEU A 41 59.828 7.743 −39.616 1.00 54.91 C ATOM 328 CD2 LEU A 41 58.320 8.338 −37.636 1.00 58.13 C ATOM 329 C LEU A 41 56.385 5.086 −38.311 1.00 55.70 C ATOM 330 O LEU A 41 56.424 4.238 −39.228 1.00 55.38 O ATOM 331 N GLY A 42 55.290 5.778 −38.001 1.00 56.61 N ATOM 332 CA GLY A 42 54.043 5.583 −38.715 1.00 57.83 C ATOM 333 C GLY A 42 53.064 4.709 −37.968 1.00 59.16 C ATOM 334 O GLY A 42 51.849 4.803 −38.199 1.00 59.45 O ATOM 335 N SER A 43 53.587 3.873 −37.060 1.00 60.41 N ATOM 336 CA SER A 43 52.775 2.988 −36.198 1.00 61.00 C ATOM 337 CB SER A 43 53.550 1.722 −35.781 1.00 60.84 C ATOM 338 OG SER A 43 53.706 0.833 −36.880 1.00 61.59 O ATOM 339 C SER A 43 52.239 3.671 −34.956 1.00 61.22 C ATOM 340 O SER A 43 52.845 4.581 −34.387 1.00 61.91 O ATOM 341 N THR A 44 51.092 3.206 −34.507 1.00 61.44 N ATOM 342 CA THR A 44 50.502 3.811 −33.352 1.00 61.38 C ATOM 343 CB THR A 44 48.964 3.869 −33.493 1.00 61.80 C ATOM 344 OG1 THR A 44 48.650 4.479 −34.762 1.00 60.23 O ATOM 345 CG2 THR A 44 48.307 4.653 −32.316 1.00 59.36 C ATOM 346 C THR A 44 50.973 3.105 −32.083 1.00 61.97 C ATOM 347 O THR A 44 51.440 3.773 −31.146 1.00 62.38 O ATOM 348 N ASN A 45 50.885 1.770 −32.064 1.00 61.54 N ATOM 349 CA ASN A 45 51.100 1.020 −30.825 1.00 61.43 C ATOM 350 CB ASN A 45 50.127 −0.173 −30.705 1.00 61.50 C ATOM 351 CG ASN A 45 48.642 0.221 −30.958 1.00 62.37 C ATOM 352 OD1 ASN A 45 48.185 1.305 −30.582 1.00 62.72 O ATOM 353 ND2 ASN A 45 47.896 −0.683 −31.590 1.00 61.46 N ATOM 354 C ASN A 45 52.560 0.609 −30.523 1.00 60.98 C ATOM 355 O ASN A 45 53.299 0.149 −31.394 1.00 61.08 O ATOM 356 N GLU A 46 52.938 0.823 −29.265 1.00 60.78 N ATOM 357 CA GLU A 46 54.210 0.400 −28.672 1.00 60.71 C ATOM 358 CB GLU A 46 54.284 0.954 −27.266 1.00 60.85 C ATOM 359 CG GLU A 46 55.575 0.708 −26.576 1.00 63.83 C ATOM 360 CD GLU A 46 55.497 1.029 −25.103 1.00 70.18 C ATOM 361 OE1 GLU A 46 54.694 0.349 −24.389 1.00 72.55 O ATOM 362 OE2 GLU A 46 56.254 1.940 −24.657 1.00 73.06 O ATOM 363 C GLU A 46 54.333 −1.121 −28.614 1.00 59.83 C ATOM 364 O GLU A 46 53.389 −1.791 −28.220 1.00 60.32 O ATOM 365 N GLN A 47 55.485 −1.669 −29.007 1.00 58.86 N ATOM 366 CA GLN A 47 55.685 −3.121 −28.999 1.00 57.92 C ATOM 367 CB GLN A 47 55.601 −3.679 −30.411 1.00 58.34 C ATOM 368 CG GLN A 47 56.948 −3.889 −31.081 1.00 61.68 C ATOM 369 CD GLN A 47 56.886 −3.720 −32.595 1.00 68.07 C ATOM 370 OE1 GLN A 47 57.774 −3.090 −33.219 1.00 69.58 O ATOM 371 NE2 GLN A 47 55.838 −4.288 −33.204 1.00 69.32 N ATOM 372 C GLN A 47 56.991 −3.546 −28.291 1.00 56.40 C ATOM 373 O GLN A 47 57.991 −2.855 −28.403 1.00 56.16 O ATOM 374 N SER A 48 56.973 −4.691 −27.599 1.00 53.86 N ATOM 375 CA SER A 48 58.112 −5.136 −26.806 1.00 53.14 C ATOM 376 CB SER A 48 57.759 −6.239 −25.793 1.00 52.59 C ATOM 377 OG SER A 48 56.373 −6.331 −25.659 1.00 55.97 O ATOM 378 C SER A 48 59.210 −5.658 −27.672 1.00 51.60 C ATOM 379 O SER A 48 58.968 −6.329 −28.679 1.00 51.19 O ATOM 380 N ILE A 49 60.433 −5.380 −27.229 1.00 50.47 N ATOM 381 CA ILE A 49 61.627 −5.856 −27.920 1.00 49.33 C ATOM 382 CB ILE A 49 62.710 −4.755 −28.005 1.00 48.45 C ATOM 383 CG1 ILE A 49 62.251 −3.636 −28.919 1.00 48.57 C ATOM 384 CD1 ILE A 49 62.995 −2.348 −28.670 1.00 47.03 C ATOM 385 CG2 ILE A 49 64.064 −5.362 −28.492 1.00 47.35 C ATOM 386 C ILE A 49 62.198 −7.054 −27.160 1.00 48.70 C ATOM 387 O ILE A 49 62.555 −6.911 −25.986 1.00 48.29 O ATOM 388 N SER A 50 62.293 −8.198 −27.849 1.00 49.00 N ATOM 389 CA SER A 50 62.998 −9.436 −27.400 1.00 49.52 C ATOM 390 CB SER A 50 62.551 −10.647 −28.223 1.00 49.72 C ATOM 391 OG SER A 50 61.213 −10.968 −27.948 1.00 52.50 O ATOM 392 C SER A 50 64.507 −9.299 −27.621 1.00 48.65 C ATOM 393 O SER A 50 64.944 −9.131 −28.735 1.00 48.05 O ATOM 394 N ILE A 51 65.270 −9.397 −26.540 1.00 47.94 N ATOM 395 CA ILE A 51 66.706 −9.224 −26.516 1.00 47.34 C ATOM 396 CB ILE A 51 67.134 −9.131 −25.012 1.00 47.28 C ATOM 397 CG1 ILE A 51 66.616 −7.835 −24.342 1.00 47.48 C ATOM 398 CD1 ILE A 51 66.759 −6.511 −25.185 1.00 46.22 C ATOM 399 CG2 ILE A 51 68.618 −9.405 −24.815 1.00 49.45 C ATOM 400 C ILE A 51 67.332 −10.427 −27.229 1.00 46.82 C ATOM 401 O ILE A 51 66.976 −11.538 −26.927 1.00 46.57 O ATOM 402 N GLY A 52 68.227 −10.219 −28.197 1.00 46.54 N ATOM 403 CA GLY A 52 68.790 −11.324 −28.979 1.00 45.30 C ATOM 404 C GLY A 52 69.129 −10.786 −30.354 1.00 46.43 C ATOM 405 O GLY A 52 68.603 −9.736 −30.754 1.00 47.18 O ATOM 406 N GLY A 53 70.047 −11.446 −31.054 1.00 45.33 N ATOM 407 CA GLY A 53 70.408 −11.065 −32.399 1.00 45.72 C ATOM 408 C GLY A 53 71.007 −9.680 −32.446 1.00 45.66 C ATOM 409 O GLY A 53 72.039 −9.435 −31.823 1.00 46.03 O ATOM 410 N ARG A 54 70.359 −8.794 −33.207 1.00 45.46 N ATOM 411 CA ARG A 54 70.681 −7.360 −33.292 1.00 45.57 C ATOM 412 CB ARG A 54 69.802 −6.697 −34.364 1.00 45.77 C ATOM 413 CG ARG A 54 70.428 −6.723 −35.756 1.00 47.80 C ATOM 414 CD ARG A 54 69.460 −6.515 −36.962 1.00 47.13 C ATOM 415 NE ARG A 54 68.139 −5.901 −36.699 1.00 48.21 N ATOM 416 CZ ARG A 54 67.854 −4.597 −36.739 1.00 48.23 C ATOM 417 NH1 ARG A 54 68.788 −3.680 −36.949 1.00 47.12 N ATOM 418 NH2 ARG A 54 66.614 −4.205 −36.539 1.00 47.74 N ATOM 419 C ARG A 54 70.538 −6.549 −31.994 1.00 44.48 C ATOM 420 O ARG A 54 71.102 −5.455 −31.899 1.00 45.01 O ATOM 421 N TYR A 55 69.760 −7.042 −31.028 1.00 43.84 N ATOM 422 CA TYR A 55 69.450 −6.305 −29.788 1.00 43.35 C ATOM 423 CB TYR A 55 67.958 −6.426 −29.448 1.00 44.35 C ATOM 424 CG TYR A 55 67.074 −5.915 −30.548 1.00 46.48 C ATOM 425 CD1 TYR A 55 66.572 −6.774 −31.512 1.00 49.83 C ATOM 426 CE1 TYR A 55 65.784 −6.314 −32.555 1.00 49.58 C ATOM 427 CZ TYR A 55 65.477 −4.973 −32.627 1.00 50.34 C ATOM 428 OH TYR A 55 64.687 −4.523 −33.663 1.00 50.81 O ATOM 429 CE2 TYR A 55 65.965 −4.079 −31.681 1.00 48.69 C ATOM 430 CD2 TYR A 55 66.772 −4.557 −30.655 1.00 48.63 C ATOM 431 C TYR A 55 70.266 −6.876 −28.651 1.00 42.80 C ATOM 432 O TYR A 55 69.952 −7.955 −28.191 1.00 42.93 O ATOM 433 N VAL A 56 71.355 −6.232 −28.240 1.00 41.64 N ATOM 434 CA VAL A 56 72.001 −6.733 −27.046 1.00 40.80 C ATOM 435 CB VAL A 56 73.464 −7.357 −27.245 1.00 42.17 C ATOM 436 CG1 VAL A 56 73.841 −7.600 −28.748 1.00 38.54 C ATOM 437 CG2 VAL A 56 74.538 −6.558 −26.522 1.00 43.83 C ATOM 438 C VAL A 56 71.827 −5.785 −25.862 1.00 41.18 C ATOM 439 O VAL A 56 71.910 −4.546 −25.990 1.00 39.41 O ATOM 440 N GLU A 57 71.512 −6.367 −24.712 1.00 40.70 N ATOM 441 CA GLU A 57 71.286 −5.580 −23.520 1.00 41.90 C ATOM 442 CB GLU A 57 69.900 −5.898 −22.929 1.00 42.24 C ATOM 443 CG GLU A 57 69.600 −5.062 −21.704 1.00 42.95 C ATOM 444 CD GLU A 57 68.308 −5.403 −20.974 1.00 42.25 C ATOM 445 OE1 GLU A 57 67.949 −6.577 −20.900 1.00 38.99 O ATOM 446 OE2 GLU A 57 67.670 −4.457 −20.460 1.00 44.79 O ATOM 447 C GLU A 57 72.384 −5.881 −22.492 1.00 42.34 C ATOM 448 O GLU A 57 72.798 −7.042 −22.344 1.00 42.11 O ATOM 449 N THR A 58 72.877 −4.831 −21.831 1.00 42.68 N ATOM 450 CA THR A 58 73.858 −4.957 −20.757 1.00 43.59 C ATOM 451 CB THR A 58 75.189 −4.212 −21.077 1.00 43.40 C ATOM 452 OG1 THR A 58 75.624 −4.579 −22.385 1.00 46.66 O ATOM 453 CG2 THR A 58 76.359 −4.628 −20.109 1.00 43.34 C ATOM 454 C THR A 58 73.158 −4.367 −19.552 1.00 44.00 C ATOM 455 O THR A 58 72.617 −3.287 −19.658 1.00 44.75 O ATOM 456 N VAL A 59 73.085 −5.096 −18.435 1.00 45.31 N ATOM 457 CA VAL A 59 72.445 −4.573 −17.188 1.00 46.32 C ATOM 458 CB VAL A 59 71.193 −5.433 −16.756 1.00 46.73 C ATOM 459 CG1 VAL A 59 70.611 −4.939 −15.416 1.00 45.96 C ATOM 460 CG2 VAL A 59 70.109 −5.392 −17.855 1.00 46.73 C ATOM 461 C VAL A 59 73.470 −4.509 −16.019 1.00 46.15 C ATOM 462 O VAL A 59 74.107 −5.492 −15.742 1.00 45.02 O ATOM 463 N ASN A 60 73.646 −3.357 −15.368 1.00 46.21 N ATOM 464 CA ASN A 60 74.410 −3.289 −14.091 1.00 47.08 C ATOM 465 CB ASN A 60 75.582 −2.282 −14.177 1.00 46.82 C ATOM 466 CG ASN A 60 76.468 −2.280 −12.923 1.00 49.00 C ATOM 467 OD1 ASN A 60 75.999 −2.345 −11.785 1.00 52.76 O ATOM 468 ND2 ASN A 60 77.757 −2.224 −13.138 1.00 49.31 N ATOM 469 C ASN A 60 73.440 −2.923 −12.955 1.00 47.32 C ATOM 470 O ASN A 60 73.134 −1.773 −12.726 1.00 46.07 O ATOM 471 N LYS A 61 72.939 −3.925 −12.255 1.00 48.72 N ATOM 472 CA LYS A 61 71.962 −3.707 −11.182 1.00 49.59 C ATOM 473 CB LYS A 61 71.378 −5.055 −10.716 1.00 49.75 C ATOM 474 CG LYS A 61 70.215 −5.564 −11.593 1.00 50.68 C ATOM 475 CD LYS A 61 69.812 −6.983 −11.174 1.00 50.86 C ATOM 476 CE LYS A 61 68.695 −7.504 −12.055 1.00 54.11 C ATOM 477 NZ LYS A 61 68.044 −8.687 −11.416 1.00 56.87 N ATOM 478 C LYS A 61 72.560 −2.919 −10.000 1.00 49.82 C ATOM 479 O LYS A 61 71.854 −2.143 −9.371 1.00 50.15 O ATOM 480 N GLY A 62 73.848 −3.134 −9.718 1.00 49.68 N ATOM 481 CA GLY A 62 74.606 −2.382 −8.706 1.00 49.85 C ATOM 482 C GLY A 62 74.552 −0.878 −8.922 1.00 49.84 C ATOM 483 O GLY A 62 74.322 −0.121 −7.980 1.00 50.26 O ATOM 484 N SER A 63 74.731 −0.433 −10.169 1.00 48.77 N ATOM 485 CA SER A 63 74.577 0.986 −10.490 1.00 47.70 C ATOM 486 CB SER A 63 75.754 1.436 −11.342 1.00 47.84 C ATOM 487 OG SER A 63 75.593 0.909 −12.632 1.00 51.09 O ATOM 488 C SER A 63 73.200 1.385 −11.111 1.00 46.97 C ATOM 489 O SER A 63 73.043 2.490 −11.649 1.00 47.21 O ATOM 490 N LYS A 64 72.209 0.497 −11.007 1.00 44.94 N ATOM 491 CA LYS A 64 70.843 0.715 −11.475 1.00 44.84 C ATOM 492 CB LYS A 64 70.057 1.625 −10.509 1.00 43.86 C ATOM 493 CG LYS A 64 70.033 1.170 −9.029 1.00 47.25 C ATOM 494 CD LYS A 64 69.005 2.001 −8.219 1.00 44.70 C ATOM 495 CE LYS A 64 69.247 1.819 −6.729 1.00 44.99 C ATOM 496 NZ LYS A 64 68.112 2.477 −6.068 1.00 44.40 N ATOM 497 C LYS A 64 70.804 1.247 −12.917 1.00 44.07 C ATOM 498 O LYS A 64 70.049 2.146 −13.280 1.00 43.97 O ATOM 499 N SER A 65 71.587 0.626 −13.752 1.00 43.50 N ATOM 500 CA SER A 65 71.940 1.168 −15.069 1.00 44.29 C ATOM 501 CB SER A 65 73.362 1.691 −14.968 1.00 44.32 C ATOM 502 OG SER A 65 73.875 1.947 −16.238 1.00 50.36 O ATOM 503 C SER A 65 71.865 0.026 −16.097 1.00 43.54 C ATOM 504 O SER A 65 72.276 −1.068 −15.818 1.00 44.78 O ATOM 505 N PHE A 66 71.310 0.273 −17.268 1.00 43.55 N ATOM 506 CA PHE A 66 71.086 −0.763 −18.282 1.00 42.34 C ATOM 507 CB PHE A 66 69.779 −1.568 −18.040 1.00 41.29 C ATOM 508 CG PHE A 66 68.550 −0.738 −17.764 1.00 43.12 C ATOM 509 CD1 PHE A 66 68.427 0.051 −16.599 1.00 42.71 C ATOM 510 CE1 PHE A 66 67.241 0.790 −16.358 1.00 44.02 C ATOM 511 CZ PHE A 66 66.195 0.688 −17.257 1.00 45.56 C ATOM 512 CE2 PHE A 66 66.300 −0.135 −18.391 1.00 43.21 C ATOM 513 CD2 PHE A 66 67.444 −0.813 −18.639 1.00 43.36 C ATOM 514 C PHE A 66 71.113 −0.110 −19.662 1.00 42.27 C ATOM 515 O PHE A 66 70.725 1.063 −19.818 1.00 40.59 O ATOM 516 N SER A 67 71.578 −0.848 −20.661 1.00 42.12 N ATOM 517 CA SER A 67 71.575 −0.287 −22.008 1.00 42.94 C ATOM 518 CB SER A 67 72.871 0.482 −22.245 1.00 44.09 C ATOM 519 OG SER A 67 73.943 −0.414 −22.195 1.00 46.13 O ATOM 520 C SER A 67 71.318 −1.326 −23.109 1.00 42.30 C ATOM 521 O SER A 67 71.475 −2.518 −22.887 1.00 41.64 O ATOM 522 N LEU A 68 70.843 −0.857 −24.259 1.00 42.72 N ATOM 523 CA LEU A 68 70.479 −1.706 −25.376 1.00 42.24 C ATOM 524 CB LEU A 68 69.032 −1.415 −25.795 1.00 42.06 C ATOM 525 CG LEU A 68 68.062 −2.356 −26.561 1.00 42.82 C ATOM 526 CD1 LEU A 68 67.123 −1.619 −27.518 1.00 37.15 C ATOM 527 CD2 LEU A 68 68.630 −3.617 −27.193 1.00 45.54 C ATOM 528 C LEU A 68 71.342 −1.215 −26.521 1.00 42.90 C ATOM 529 O LEU A 68 71.347 −0.010 −26.820 1.00 41.46 O ATOM 530 N ARG A 69 72.031 −2.141 −27.196 1.00 42.96 N ATOM 531 CA ARG A 69 72.635 −1.810 −28.465 1.00 43.33 C ATOM 532 CB ARG A 69 74.071 −2.295 −28.521 1.00 44.06 C ATOM 533 CG ARG A 69 74.908 −1.467 −29.419 1.00 44.93 C ATOM 534 CD ARG A 69 76.347 −1.648 −29.074 1.00 51.01 C ATOM 535 NE ARG A 69 77.032 −2.495 −30.046 1.00 55.03 N ATOM 536 CZ ARG A 69 77.938 −2.041 −30.924 1.00 59.47 C ATOM 537 NH1 ARG A 69 78.259 −0.733 −30.942 1.00 59.92 N ATOM 538 NH2 ARG A 69 78.520 −2.876 −31.794 1.00 52.94 N ATOM 539 C ARG A 69 71.867 −2.458 −29.589 1.00 43.41 C ATOM 540 O ARG A 69 71.684 −3.661 −29.590 1.00 42.37 O ATOM 541 N ILE A 70 71.416 −1.646 −30.545 1.00 43.65 N ATOM 542 CA ILE A 70 70.858 −2.153 −31.779 1.00 44.23 C ATOM 543 CB ILE A 70 69.492 −1.515 −32.157 1.00 44.17 C ATOM 544 CG1 ILE A 70 68.603 −1.333 −30.942 1.00 45.74 C ATOM 545 CD1 ILE A 70 67.758 −0.131 −31.117 1.00 46.30 C ATOM 546 CG2 ILE A 70 68.756 −2.351 −33.172 1.00 43.47 C ATOM 547 C ILE A 70 71.856 −1.934 −32.893 1.00 44.58 C ATOM 548 O ILE A 70 72.153 −0.792 −33.282 1.00 45.70 O ATOM 549 N SER A 71 72.376 −3.022 −33.425 1.00 45.40 N ATOM 550 CA SER A 71 73.387 −2.879 −34.435 1.00 46.26 C ATOM 551 CB SER A 71 74.597 −3.736 −34.104 1.00 46.66 C ATOM 552 OG SER A 71 74.223 −5.080 −34.154 1.00 46.90 O ATOM 553 C SER A 71 72.788 −3.238 −35.776 1.00 46.26 C ATOM 554 O SER A 71 71.702 −3.811 −35.833 1.00 45.27 O ATOM 555 N ASP A 72 73.491 −2.855 −36.845 1.00 47.04 N ATOM 556 CA ASP A 72 73.083 −3.164 −38.220 1.00 47.40 C ATOM 557 CB ASP A 72 73.125 −4.671 −38.470 1.00 47.74 C ATOM 558 CG ASP A 72 73.180 −5.019 −39.934 1.00 51.59 C ATOM 559 OD1 ASP A 72 73.693 −4.202 −40.771 1.00 53.46 O ATOM 560 OD2 ASP A 72 72.705 −6.140 −40.238 1.00 56.93 O ATOM 561 C ASP A 72 71.704 −2.556 −38.534 1.00 46.75 C ATOM 562 O ASP A 72 70.796 −3.217 −39.079 1.00 46.48 O ATOM 563 N LEU A 73 71.601 −1.275 −38.183 1.00 46.13 N ATOM 564 CA LEU A 73 70.406 −0.467 −38.296 1.00 45.96 C ATOM 565 CB LEU A 73 70.745 0.931 −37.780 1.00 45.33 C ATOM 566 CG LEU A 73 70.287 1.479 −36.425 1.00 48.34 C ATOM 567 CD1 LEU A 73 69.586 0.448 −35.493 1.00 42.67 C ATOM 568 CD2 LEU A 73 71.423 2.297 −35.755 1.00 49.05 C ATOM 569 C LEU A 73 69.946 −0.366 −39.742 1.00 46.10 C ATOM 570 O LEU A 73 70.764 −0.352 −40.660 1.00 44.78 O ATOM 571 N ARG A 74 68.631 −0.281 −39.934 1.00 46.57 N ATOM 572 CA ARG A 74 68.040 −0.106 −41.264 1.00 47.37 C ATOM 573 CB ARG A 74 67.637 −1.474 −41.849 1.00 46.77 C ATOM 574 CG ARG A 74 66.719 −2.239 −40.899 1.00 49.24 C ATOM 575 CD ARG A 74 66.663 −3.759 −41.079 1.00 50.32 C ATOM 576 NE ARG A 74 67.971 −4.409 −40.931 1.00 53.80 N ATOM 577 CZ ARG A 74 68.136 −5.671 −40.534 1.00 55.17 C ATOM 578 NH1 ARG A 74 67.079 −6.433 −40.214 1.00 53.89 N ATOM 579 NH2 ARG A 74 69.367 −6.169 −40.440 1.00 55.31 N ATOM 580 C ARG A 74 66.851 0.854 −41.114 1.00 46.54 C ATOM 581 O ARG A 74 66.367 1.069 −39.989 1.00 46.24 O ATOM 582 N VAL A 75 66.407 1.456 −42.221 1.00 46.74 N ATOM 583 CA VAL A 75 65.304 2.453 −42.211 1.00 47.37 C ATOM 584 CB VAL A 75 64.850 2.870 −43.638 1.00 47.20 C ATOM 585 CG1 VAL A 75 63.727 3.897 −43.563 1.00 48.39 C ATOM 586 CG2 VAL A 75 65.979 3.477 −44.373 1.00 45.91 C ATOM 587 C VAL A 75 64.073 2.053 −41.387 1.00 47.49 C ATOM 588 O VAL A 75 63.434 2.919 −40.786 1.00 48.41 O ATOM 589 N GLU A 76 63.774 0.748 −41.340 1.00 47.38 N ATOM 590 CA GLU A 76 62.578 0.186 −40.682 1.00 47.03 C ATOM 591 CB GLU A 76 62.327 −1.264 −41.122 1.00 46.90 C ATOM 592 CG GLU A 76 62.075 −1.440 −42.631 1.00 50.85 C ATOM 593 CD GLU A 76 63.370 −1.574 −43.459 1.00 56.49 C ATOM 594 OE1 GLU A 76 64.438 −1.844 −42.855 1.00 56.84 O ATOM 595 OE2 GLU A 76 63.321 −1.414 −44.721 1.00 60.06 O ATOM 596 C GLU A 76 62.681 0.239 −39.173 1.00 46.09 C ATOM 597 O GLU A 76 61.694 0.020 −38.485 1.00 46.19 O ATOM 598 N ASP A 77 63.880 0.526 −38.662 1.00 45.73 N ATOM 599 CA ASP A 77 64.123 0.677 −37.224 1.00 44.49 C ATOM 600 CB ASP A 77 65.557 0.277 −36.855 1.00 44.34 C ATOM 601 CG ASP A 77 65.839 −1.207 −37.086 1.00 47.06 C ATOM 602 OD1 ASP A 77 64.964 −2.086 −36.810 1.00 51.98 O ATOM 603 OD2 ASP A 77 66.959 −1.515 −37.546 1.00 50.67 O ATOM 604 C ASP A 77 63.820 2.086 −36.705 1.00 44.17 C ATOM 605 O ASP A 77 63.795 2.288 −35.501 1.00 43.66 O ATOM 606 N SER A 78 63.606 3.056 −37.601 1.00 43.76 N ATOM 607 CA SER A 78 63.254 4.403 −37.176 1.00 43.69 C ATOM 608 CB SER A 78 62.975 5.334 −38.352 1.00 43.43 C ATOM 609 OG SER A 78 64.074 5.409 −39.232 1.00 42.84 O ATOM 610 C SER A 78 62.026 4.342 −36.304 1.00 44.36 C ATOM 611 O SER A 78 61.112 3.604 −36.591 1.00 45.78 O ATOM 612 N GLY A 79 62.009 5.134 −35.239 1.00 44.36 N ATOM 613 CA GLY A 79 60.931 5.138 −34.284 1.00 43.30 C ATOM 614 C GLY A 79 61.435 5.586 −32.936 1.00 43.00 C ATOM 615 O GLY A 79 62.541 6.110 −32.830 1.00 43.25 O ATOM 616 N THR A 80 60.585 5.415 −31.929 1.00 42.21 N ATOM 617 CA THR A 80 60.837 5.861 −30.587 1.00 42.60 C ATOM 618 CB THR A 80 59.658 6.697 −30.047 1.00 43.53 C ATOM 619 OG1 THR A 80 59.501 7.860 −30.873 1.00 45.61 O ATOM 620 CG2 THR A 80 59.869 7.123 −28.565 1.00 44.78 C ATOM 621 C THR A 80 61.047 4.587 −29.775 1.00 42.21 C ATOM 622 O THR A 80 60.308 3.637 −29.924 1.00 41.06 O ATOM 623 N TYR A 81 62.115 4.578 −28.973 1.00 41.77 N ATOM 624 CA TYR A 81 62.463 3.459 −28.122 1.00 40.78 C ATOM 625 CB TYR A 81 63.891 2.998 −28.407 1.00 39.74 C ATOM 626 CG TYR A 81 64.031 2.350 −29.774 1.00 40.54 C ATOM 627 CD1 TYR A 81 64.286 0.993 −29.909 1.00 38.77 C ATOM 628 CE1 TYR A 81 64.400 0.414 −31.226 1.00 42.36 C ATOM 629 CZ TYR A 81 64.245 1.208 −32.347 1.00 37.03 C ATOM 630 OH TYR A 81 64.353 0.685 −33.633 1.00 39.33 O ATOM 631 CE2 TYR A 81 63.975 2.523 −32.218 1.00 38.69 C ATOM 632 CD2 TYR A 81 63.891 3.106 −30.932 1.00 40.06 C ATOM 633 C TYR A 81 62.382 3.935 −26.715 1.00 40.90 C ATOM 634 O TYR A 81 62.766 5.033 −26.462 1.00 40.58 O ATOM 635 N LYS A 82 61.896 3.088 −25.819 1.00 41.29 N ATOM 636 CA LYS A 82 61.850 3.350 −24.388 1.00 42.71 C ATOM 637 CB LYS A 82 60.422 3.634 −23.944 1.00 42.24 C ATOM 638 CG LYS A 82 59.994 4.963 −24.379 1.00 44.27 C ATOM 639 CD LYS A 82 58.731 5.424 −23.596 1.00 45.18 C ATOM 640 CE LYS A 82 58.202 6.727 −24.265 1.00 46.00 C ATOM 641 NZ LYS A 82 57.117 7.194 −23.357 1.00 56.94 N ATOM 642 C LYS A 82 62.315 2.107 −23.650 1.00 42.18 C ATOM 643 O LYS A 82 62.061 1.027 −24.094 1.00 40.76 O ATOM 644 N CYS A 83 63.042 2.318 −22.560 1.00 43.46 N ATOM 645 CA CYS A 83 63.439 1.309 −21.629 1.00 44.61 C ATOM 646 CB CYS A 83 64.761 1.693 −20.986 1.00 45.96 C ATOM 647 SG CYS A 83 64.973 3.375 −20.311 1.00 48.94 S ATOM 648 C CYS A 83 62.409 1.325 −20.534 1.00 45.71 C ATOM 649 O CYS A 83 61.631 2.271 −20.456 1.00 46.30 O ATOM 650 N GLN A 84 62.385 0.287 −19.692 1.00 43.77 N ATOM 651 CA GLN A 84 61.568 0.350 −18.534 1.00 42.92 C ATOM 652 CB GLN A 84 60.203 −0.292 −18.790 1.00 42.16 C ATOM 653 CG GLN A 84 59.330 −0.191 −17.551 1.00 43.09 C ATOM 654 CD GLN A 84 57.821 −0.376 −17.766 1.00 46.36 C ATOM 655 OE1 GLN A 84 57.016 0.257 −17.094 1.00 50.63 O ATOM 656 NE2 GLN A 84 57.443 −1.260 −18.660 1.00 44.97 N ATOM 657 C GLN A 84 62.286 −0.351 −17.413 1.00 42.33 C ATOM 658 O GLN A 84 62.766 −1.454 −17.614 1.00 40.11 O ATOM 659 N ALA A 85 62.403 0.310 −16.256 1.00 42.76 N ATOM 660 CA ALA A 85 62.992 −0.323 −15.027 1.00 43.66 C ATOM 661 CB ALA A 85 63.803 0.674 −14.213 1.00 42.44 C ATOM 662 C ALA A 85 61.854 −0.875 −14.159 1.00 43.77 C ATOM 663 O ALA A 85 60.904 −0.143 −13.877 1.00 42.85 O ATOM 664 N PHE A 86 61.986 −2.140 −13.760 1.00 42.59 N ATOM 665 CA PHE A 86 61.015 −2.843 −12.918 1.00 43.37 C ATOM 666 CB PHE A 86 60.674 −4.222 −13.484 1.00 41.48 C ATOM 667 CG PHE A 86 60.048 −4.178 −14.879 1.00 43.52 C ATOM 668 CD1 PHE A 86 58.751 −3.695 −15.063 1.00 40.20 C ATOM 669 CE1 PHE A 86 58.158 −3.672 −16.327 1.00 38.57 C ATOM 670 CZ PHE A 86 58.871 −4.088 −17.428 1.00 42.08 C ATOM 671 CE2 PHE A 86 60.178 −4.538 −17.273 1.00 43.63 C ATOM 672 CD2 PHE A 86 60.765 −4.568 −15.998 1.00 42.39 C ATOM 673 C PHE A 86 61.564 −2.990 −11.487 1.00 44.25 C ATOM 674 O PHE A 86 62.745 −3.227 −11.275 1.00 45.17 O ATOM 675 N TYR A 87 60.673 −2.891 −10.514 1.00 44.26 N ATOM 676 CA TYR A 87 61.056 −2.955 −9.127 1.00 42.81 C ATOM 677 CB TYR A 87 61.591 −1.595 −8.705 1.00 42.95 C ATOM 678 CG TYR A 87 60.589 −0.506 −9.034 1.00 44.84 C ATOM 679 CD1 TYR A 87 60.593 0.094 −10.300 1.00 44.05 C ATOM 680 CE1 TYR A 87 59.685 1.047 −10.640 1.00 46.61 C ATOM 681 CZ TYR A 87 58.730 1.425 −9.702 1.00 45.72 C ATOM 682 OH TYR A 87 57.877 2.355 −10.081 1.00 48.88 O ATOM 683 CE2 TYR A 87 58.659 0.878 −8.442 1.00 45.57 C ATOM 684 CD2 TYR A 87 59.622 −0.126 −8.110 1.00 45.85 C ATOM 685 C TYR A 87 59.820 −3.359 −8.308 1.00 42.27 C ATOM 686 O TYR A 87 58.694 −3.482 −8.832 1.00 42.84 O ATOM 687 N VAL A 88 60.017 −3.599 −7.022 1.00 41.80 N ATOM 688 CA VAL A 88 58.912 −3.966 −6.147 1.00 40.05 C ATOM 689 CB VAL A 88 59.180 −5.357 −5.568 1.00 40.65 C ATOM 690 CG1 VAL A 88 60.622 −5.432 −4.904 1.00 34.41 C ATOM 691 CG2 VAL A 88 59.093 −6.416 −6.658 1.00 36.97 C ATOM 692 C VAL A 88 58.720 −2.893 −5.015 1.00 41.14 C ATOM 693 O VAL A 88 59.646 −2.140 −4.619 1.00 42.19 O ATOM 694 N PHE A 89 57.529 −2.846 −4.472 1.00 40.69 N ATOM 695 CA PHE A 89 57.239 −1.957 −3.367 1.00 38.05 C ATOM 696 CB PHE A 89 57.064 −0.483 −3.841 1.00 37.66 C ATOM 697 CG PHE A 89 55.841 −0.218 −4.771 1.00 35.47 C ATOM 698 CD1 PHE A 89 55.948 −0.343 −6.141 1.00 34.15 C ATOM 699 CE1 PHE A 89 54.868 −0.074 −6.984 1.00 30.34 C ATOM 700 CZ PHE A 89 53.716 0.379 −6.408 1.00 38.20 C ATOM 701 CE2 PHE A 89 53.627 0.586 −4.999 1.00 30.74 C ATOM 702 CD2 PHE A 89 54.662 0.290 −4.241 1.00 36.54 C ATOM 703 C PHE A 89 56.012 −2.518 −2.694 1.00 39.07 C ATOM 704 O PHE A 89 55.218 −3.234 −3.341 1.00 35.78 O ATOM 705 N PHE A 90 55.886 −2.215 −1.394 1.00 38.51 N ATOM 706 CA PHE A 90 54.693 −2.576 −0.621 1.00 39.88 C ATOM 707 CB PHE A 90 54.993 −2.528 0.874 1.00 37.98 C ATOM 708 CG PHE A 90 55.700 −3.740 1.386 1.00 37.62 C ATOM 709 CD1 PHE A 90 55.078 −5.003 1.336 1.00 35.79 C ATOM 710 CE1 PHE A 90 55.688 −6.126 1.895 1.00 37.83 C ATOM 711 CZ PHE A 90 56.950 −6.030 2.476 1.00 38.12 C ATOM 712 CE2 PHE A 90 57.601 −4.739 2.526 1.00 38.60 C ATOM 713 CD2 PHE A 90 56.922 −3.620 1.998 1.00 37.29 C ATOM 714 C PHE A 90 53.467 −1.698 −0.981 1.00 40.53 C ATOM 715 O PHE A 90 53.605 −0.502 −1.196 1.00 40.32 O ATOM 716 N ALA A 91 52.277 −2.306 −0.985 1.00 41.27 N ATOM 717 CA ALA A 91 51.067 −1.617 −1.372 1.00 41.84 C ATOM 718 CB ALA A 91 49.892 −2.513 −1.182 1.00 42.15 C ATOM 719 C ALA A 91 50.860 −0.249 −0.668 1.00 43.70 C ATOM 720 O ALA A 91 50.328 0.664 −1.280 1.00 43.35 O ATOM 721 N GLU A 92 51.321 −0.091 0.581 1.00 44.95 N ATOM 722 CA GLU A 92 51.195 1.188 1.293 1.00 45.93 C ATOM 723 CB GLU A 92 50.780 0.942 2.711 1.00 46.65 C ATOM 724 CG GLU A 92 49.555 0.079 2.779 1.00 48.11 C ATOM 725 CD GLU A 92 48.913 0.127 4.131 1.00 57.18 C ATOM 726 OE1 GLU A 92 48.562 1.252 4.563 1.00 59.80 O ATOM 727 OE2 GLU A 92 48.750 −0.953 4.764 1.00 56.56 O ATOM 728 C GLU A 92 52.446 2.067 1.252 1.00 47.30 C ATOM 729 O GLU A 92 52.450 3.195 1.756 1.00 48.77 O ATOM 730 N ASP A 93 53.503 1.616 0.598 1.00 46.55 N ATOM 731 CA ASP A 93 54.636 2.501 0.483 1.00 46.41 C ATOM 732 CB ASP A 93 55.884 1.692 0.182 1.00 45.51 C ATOM 733 CG ASP A 93 57.082 2.561 −0.131 1.00 44.76 C ATOM 734 OD1 ASP A 93 58.026 2.046 −0.789 1.00 42.86 O ATOM 735 OD2 ASP A 93 57.072 3.754 0.253 1.00 42.99 O ATOM 736 C ASP A 93 54.344 3.551 −0.605 1.00 46.69 C ATOM 737 O ASP A 93 54.653 3.334 −1.774 1.00 46.46 O ATOM 738 N VAL A 94 53.716 4.660 −0.218 1.00 46.68 N ATOM 739 CA VAL A 94 53.276 5.672 −1.199 1.00 47.78 C ATOM 740 CB VAL A 94 52.240 6.690 −0.629 1.00 47.50 C ATOM 741 CG1 VAL A 94 52.844 7.591 0.471 1.00 48.03 C ATOM 742 CG2 VAL A 94 51.023 5.941 −0.088 1.00 48.45 C ATOM 743 C VAL A 94 54.439 6.375 −1.893 1.00 47.62 C ATOM 744 O VAL A 94 54.323 6.822 −3.039 1.00 48.80 O ATOM 745 N GLY A 95 55.577 6.444 −1.228 1.00 47.46 N ATOM 746 CA GLY A 95 56.743 7.084 −1.829 1.00 46.54 C ATOM 747 C GLY A 95 57.216 6.371 −3.077 1.00 46.80 C ATOM 748 O GLY A 95 57.971 6.944 −3.858 1.00 48.77 O ATOM 749 N SER A 96 56.789 5.125 −3.282 1.00 45.12 N ATOM 750 CA SER A 96 57.316 4.299 −4.367 1.00 43.91 C ATOM 751 CB SER A 96 57.806 2.951 −3.774 1.00 43.86 C ATOM 752 OG SER A 96 59.082 3.050 −3.170 1.00 45.47 O ATOM 753 C SER A 96 56.280 3.976 −5.464 1.00 43.04 C ATOM 754 O SER A 96 56.556 3.141 −6.333 1.00 41.97 O ATOM 755 N ASN A 97 55.083 4.582 −5.411 1.00 42.62 N ATOM 756 CA ASN A 97 53.955 4.125 −6.262 1.00 41.42 C ATOM 757 CB ASN A 97 52.664 3.995 −5.411 1.00 41.08 C ATOM 758 CG ASN A 97 52.129 5.344 −4.941 1.00 42.94 C ATOM 759 OD1 ASN A 97 52.503 6.365 −5.465 1.00 46.83 O ATOM 760 ND2 ASN A 97 51.255 5.342 −3.965 1.00 40.83 N ATOM 761 C ASN A 97 53.666 4.932 −7.525 1.00 42.28 C ATOM 762 O ASN A 97 52.585 4.750 −8.141 1.00 41.82 O ATOM 763 N LYS A 98 54.573 5.850 −7.915 1.00 42.02 N ATOM 764 CA LYS A 98 54.248 6.732 −9.041 1.00 43.43 C ATOM 765 CB LYS A 98 54.942 8.098 −8.900 1.00 44.23 C ATOM 766 CG LYS A 98 55.210 8.508 −7.418 1.00 46.17 C ATOM 767 CD LYS A 98 54.021 9.049 −6.764 1.00 48.50 C ATOM 768 CE LYS A 98 54.408 9.875 −5.559 1.00 45.50 C ATOM 769 NZ LYS A 98 54.697 8.979 −4.390 1.00 48.43 N ATOM 770 C LYS A 98 54.460 6.112 −10.439 1.00 43.17 C ATOM 771 O LYS A 98 54.025 6.663 −11.415 1.00 42.52 O ATOM 772 N GLY A 99 55.057 4.929 −10.498 1.00 43.81 N ATOM 773 CA GLY A 99 55.295 4.242 −11.742 1.00 43.60 C ATOM 774 C GLY A 99 54.052 3.507 −12.181 1.00 42.19 C ATOM 775 O GLY A 99 53.008 3.607 −11.544 1.00 42.85 O ATOM 776 N ALA A 100 54.151 2.775 −13.283 1.00 40.39 N ATOM 777 CA ALA A 100 53.014 1.974 −13.753 1.00 39.22 C ATOM 778 CB ALA A 100 53.278 1.513 −15.205 1.00 36.47 C ATOM 779 C ALA A 100 52.932 0.751 −12.819 1.00 38.50 C ATOM 780 O ALA A 100 53.913 0.368 −12.262 1.00 38.16 O ATOM 781 N ILE A 101 51.772 0.140 −12.652 1.00 38.62 N ATOM 782 CA ILE A 101 51.638 −1.134 −11.945 1.00 38.55 C ATOM 783 CB ILE A 101 50.190 −1.269 −11.405 1.00 40.06 C ATOM 784 CG1 ILE A 101 49.797 0.015 −10.598 1.00 42.79 C ATOM 785 CD1 ILE A 101 50.554 0.261 −9.310 1.00 39.48 C ATOM 786 CG2 ILE A 101 49.959 −2.667 −10.762 1.00 36.33 C ATOM 787 C ILE A 101 51.767 −2.274 −12.951 1.00 39.19 C ATOM 788 O ILE A 101 50.995 −2.357 −13.950 1.00 36.64 O ATOM 789 N ILE A 102 52.677 −3.191 −12.663 1.00 39.81 N ATOM 790 CA ILE A 102 52.909 −4.348 −13.578 1.00 39.64 C ATOM 791 CB ILE A 102 54.454 −4.487 −13.734 1.00 39.59 C ATOM 792 CG1 ILE A 102 55.089 −3.117 −14.157 1.00 38.41 C ATOM 793 CD1 ILE A 102 54.460 −2.524 −15.511 1.00 33.86 C ATOM 794 CG2 ILE A 102 54.819 −5.583 −14.725 1.00 40.76 C ATOM 795 C ILE A 102 52.195 −5.647 −13.073 1.00 39.13 C ATOM 796 O ILE A 102 51.854 −6.530 −13.816 1.00 39.94 O ATOM 797 N GLY A 103 52.050 −5.776 −11.775 1.00 39.01 N ATOM 798 CA GLY A 103 51.334 −6.885 −11.213 1.00 38.49 C ATOM 799 C GLY A 103 51.324 −6.752 −9.716 1.00 37.24 C ATOM 800 O GLY A 103 51.882 −5.833 −9.130 1.00 36.17 O ATOM 801 N LEU A 104 50.749 −7.742 −9.089 1.00 37.99 N ATOM 802 CA LEU A 104 50.493 −7.683 −7.688 1.00 39.66 C ATOM 803 CB LEU A 104 49.031 −7.210 −7.355 1.00 37.53 C ATOM 804 CG LEU A 104 48.649 −7.290 −5.842 1.00 40.70 C ATOM 805 CD1 LEU A 104 47.171 −7.118 −5.505 1.00 39.27 C ATOM 806 CD2 LEU A 104 49.430 −6.275 −4.991 1.00 38.45 C ATOM 807 C LEU A 104 50.744 −9.080 −7.236 1.00 40.91 C ATOM 808 O LEU A 104 50.123 −10.019 −7.747 1.00 40.88 O ATOM 809 N MET A 105 51.687 −9.213 −6.306 1.00 43.27 N ATOM 810 CA MET A 105 51.982 −10.471 −5.649 1.00 45.57 C ATOM 811 CB MET A 105 53.480 −10.581 −5.502 1.00 47.53 C ATOM 812 CG MET A 105 54.143 −11.586 −6.445 1.00 56.01 C ATOM 813 SD MET A 105 53.858 −11.477 −8.250 1.00 66.51 S ATOM 814 CE MET A 105 54.839 −12.860 −8.841 1.00 57.93 C ATOM 815 C MET A 105 51.291 −10.529 −4.289 1.00 44.27 C ATOM 816 O MET A 105 51.143 −9.509 −3.650 1.00 43.68 O ATOM 817 N VAL A 106 50.826 −11.700 −3.870 1.00 44.78 N ATOM 818 CA VAL A 106 50.387 −11.916 −2.462 1.00 46.00 C ATOM 819 CB VAL A 106 50.185 −13.396 −2.124 1.00 46.66 C ATOM 820 CG1 VAL A 106 51.551 −14.154 −2.328 1.00 47.69 C ATOM 821 CG2 VAL A 106 49.015 −13.959 −2.921 1.00 45.00 C ATOM 822 C VAL A 106 51.431 −11.451 −1.442 1.00 46.49 C ATOM 823 O VAL A 106 52.639 −11.733 −1.590 1.00 46.05 O ATOM 824 N GLY A 107 50.942 −10.795 −0.390 1.00 45.74 N ATOM 825 CA GLY A 107 51.799 −10.227 0.629 1.00 44.85 C ATOM 826 C GLY A 107 51.784 −8.730 0.425 1.00 44.68 C ATOM 827 O GLY A 107 52.526 −8.029 1.054 1.00 45.42 O ATOM 828 N GLY A 108 50.939 −8.247 −0.480 1.00 43.98 N ATOM 829 CA GLY A 108 50.840 −6.821 −0.790 1.00 43.08 C ATOM 830 C GLY A 108 52.084 −6.255 −1.442 1.00 42.91 C ATOM 831 O GLY A 108 52.434 −5.089 −1.242 1.00 42.44 O ATOM 832 N VAL A 109 52.719 −7.046 −2.291 1.00 43.26 N ATOM 833 CA VAL A 109 53.948 −6.599 −2.957 1.00 42.66 C ATOM 834 CB VAL A 109 55.000 −7.751 −2.883 1.00 43.69 C ATOM 835 CG1 VAL A 109 56.193 −7.522 −3.854 1.00 42.19 C ATOM 836 CG2 VAL A 109 55.408 −8.004 −1.423 1.00 42.91 C ATOM 837 C VAL A 109 53.554 −6.242 −4.387 1.00 42.97 C ATOM 838 O VAL A 109 53.096 −7.113 −5.167 1.00 42.03 O ATOM 839 N VAL A 110 53.665 −4.958 −4.723 1.00 42.17 N ATOM 840 CA VAL A 110 53.415 −4.541 −6.054 1.00 40.80 C ATOM 841 CB VAL A 110 52.310 −3.424 −6.153 1.00 44.02 C ATOM 842 CG1 VAL A 110 52.372 −2.549 −7.365 1.00 42.03 C ATOM 843 CG2 VAL A 110 51.848 −2.769 −4.779 1.00 41.33 C ATOM 844 C VAL A 110 54.630 −4.554 −6.979 1.00 41.32 C ATOM 845 O VAL A 110 55.745 −4.275 −6.542 1.00 41.11 O ATOM 846 N ILE A 111 54.454 −4.937 −8.242 1.00 40.50 N ATOM 847 CA ILE A 111 55.520 −4.758 −9.218 1.00 39.74 C ATOM 848 CB ILE A 111 55.693 −6.002 −10.151 1.00 42.13 C ATOM 849 CG1 ILE A 111 55.947 −7.264 −9.286 1.00 44.65 C ATOM 850 CD1 ILE A 111 55.492 −8.577 −9.969 1.00 51.14 C ATOM 851 CG2 ILE A 111 56.814 −5.793 −11.241 1.00 39.84 C ATOM 852 C ILE A 111 55.308 −3.462 −9.981 1.00 38.67 C ATOM 853 O ILE A 111 54.231 −3.209 −10.519 1.00 39.08 O ATOM 854 N GLY A 112 56.314 −2.594 −9.989 1.00 37.53 N ATOM 855 CA GLY A 112 56.135 −1.251 −10.626 1.00 36.49 C ATOM 856 C GLY A 112 57.100 −1.138 −11.758 1.00 37.46 C ATOM 857 O GLY A 112 58.065 −1.929 −11.859 1.00 37.41 O ATOM 858 N GLY A 113 56.787 −0.246 −12.688 1.00 38.41 N ATOM 859 CA GLY A 113 57.674 0.011 −13.832 1.00 39.24 C ATOM 860 C GLY A 113 57.818 1.473 −14.008 1.00 38.63 C ATOM 861 O GLY A 113 56.810 2.152 −13.932 1.00 40.39 O ATOM 862 N GLU A 114 59.046 1.981 −14.149 1.00 40.63 N ATOM 863 CA GLU A 114 59.293 3.395 −14.613 1.00 42.64 C ATOM 864 CB GLU A 114 60.340 4.176 −13.800 1.00 42.87 C ATOM 865 CG GLU A 114 59.955 4.975 −12.595 1.00 50.17 C ATOM 866 CD GLU A 114 58.981 6.134 −12.814 1.00 55.34 C ATOM 867 OE1 GLU A 114 59.160 6.926 −13.769 1.00 61.09 O ATOM 868 OE2 GLU A 114 58.080 6.310 −11.959 1.00 57.31 O ATOM 869 C GLU A 114 59.949 3.324 −15.964 1.00 42.42 C ATOM 870 O GLU A 114 60.953 2.626 −16.132 1.00 43.93 O ATOM 871 N LYS A 115 59.503 4.152 −16.876 1.00 42.38 N ATOM 872 CA LYS A 115 60.016 4.192 −18.240 1.00 42.73 C ATOM 873 CB LYS A 115 58.829 4.219 −19.234 1.00 44.06 C ATOM 874 CG LYS A 115 58.069 2.975 −19.365 1.00 47.53 C ATOM 875 CD LYS A 115 57.203 3.006 −20.629 1.00 53.24 C ATOM 876 CE LYS A 115 56.289 1.786 −20.589 1.00 54.45 C ATOM 877 NZ LYS A 115 55.402 1.783 −21.803 1.00 61.37 N ATOM 878 C LYS A 115 60.796 5.484 −18.507 1.00 41.16 C ATOM 879 O LYS A 115 60.463 6.586 −18.007 1.00 40.33 O ATOM 880 N GLY A 116 61.804 5.356 −19.341 1.00 40.59 N ATOM 881 CA GLY A 116 62.579 6.518 −19.817 1.00 39.49 C ATOM 882 C GLY A 116 61.717 7.400 −20.692 1.00 40.21 C ATOM 883 O GLY A 116 60.615 6.997 −21.112 1.00 38.64 O ATOM 884 N ALA A 117 62.212 8.605 −20.987 1.00 41.52 N ATOM 885 CA ALA A 117 61.472 9.547 −21.817 1.00 42.80 C ATOM 886 CB ALA A 117 62.048 10.974 −21.662 1.00 44.34 C ATOM 887 C ALA A 117 61.451 9.187 −23.295 1.00 43.54 C ATOM 888 O ALA A 117 60.687 9.767 −24.039 1.00 44.55 O ATOM 889 N GLY A 118 62.303 8.280 −23.760 1.00 43.70 N ATOM 890 CA GLY A 118 62.260 7.966 −25.184 1.00 41.16 C ATOM 891 C GLY A 118 63.528 8.367 −25.883 1.00 41.11 C ATOM 892 O GLY A 118 64.195 9.321 −25.473 1.00 41.17 O ATOM 893 N THR A 119 63.870 7.617 −26.927 1.00 40.36 N ATOM 894 CA THR A 119 64.921 7.982 −27.896 1.00 39.93 C ATOM 895 CB THR A 119 66.082 6.926 −27.933 1.00 39.67 C ATOM 896 OG1 THR A 119 66.775 6.941 −26.682 1.00 36.77 O ATOM 897 CG2 THR A 119 67.130 7.237 −29.078 1.00 37.93 C ATOM 898 C THR A 119 64.168 7.915 −29.198 1.00 40.54 C ATOM 899 O THR A 119 63.610 6.841 −29.510 1.00 41.01 O ATOM 900 N ALA A 120 64.042 9.058 −29.886 1.00 39.18 N ATOM 901 CA ALA A 120 63.474 9.123 −31.240 1.00 39.16 C ATOM 902 CB ALA A 120 62.887 10.544 −31.521 1.00 39.16 C ATOM 903 C ALA A 120 64.617 8.819 −32.234 1.00 38.85 C ATOM 904 O ALA A 120 65.576 9.562 −32.300 1.00 37.63 O ATOM 905 N LEU A 121 64.560 7.680 −32.925 1.00 39.42 N ATOM 906 CA LEU A 121 65.634 7.279 −33.798 1.00 39.83 C ATOM 907 CB LEU A 121 66.049 5.819 −33.513 1.00 40.42 C ATOM 908 CG LEU A 121 66.974 5.144 −34.569 1.00 40.59 C ATOM 909 CD1 LEU A 121 68.396 5.751 −34.587 1.00 38.95 C ATOM 910 CD2 LEU A 121 67.007 3.604 −34.288 1.00 41.03 C ATOM 911 C LEU A 121 65.256 7.492 −35.280 1.00 40.22 C ATOM 912 O LEU A 121 64.147 7.165 −35.705 1.00 39.00 O ATOM 913 N THR A 122 66.171 8.081 −36.057 1.00 40.54 N ATOM 914 CA THR A 122 65.968 8.199 −37.476 1.00 40.45 C ATOM 915 CB THR A 122 65.896 9.701 −37.936 1.00 41.48 C ATOM 916 OG1 THR A 122 64.702 10.294 −37.406 1.00 44.87 O ATOM 917 CG2 THR A 122 65.878 9.852 −39.480 1.00 39.71 C ATOM 918 C THR A 122 67.138 7.487 −38.092 1.00 40.29 C ATOM 919 O THR A 122 68.279 7.874 −37.877 1.00 39.60 O ATOM 920 N VAL A 123 66.875 6.408 −38.818 1.00 40.92 N ATOM 921 CA VAL A 123 67.930 5.869 −39.707 1.00 41.20 C ATOM 922 CB VAL A 123 68.359 4.405 −39.388 1.00 41.03 C ATOM 923 CG1 VAL A 123 67.511 3.799 −38.233 1.00 39.09 C ATOM 924 CG2 VAL A 123 68.518 3.549 −40.620 1.00 40.22 C ATOM 925 C VAL A 123 67.788 6.260 −41.186 1.00 42.10 C ATOM 926 O VAL A 123 66.767 6.047 −41.842 1.00 42.13 O ATOM 927 N LYS A 124 68.836 6.892 −41.677 1.00 43.39 N ATOM 928 CA LYS A 124 68.864 7.415 −43.030 1.00 44.97 C ATOM 929 CB LYS A 124 70.047 8.388 −43.187 1.00 44.33 C ATOM 930 CG LYS A 124 69.902 9.697 −42.471 1.00 43.86 C ATOM 931 CD LYS A 124 71.265 10.355 −42.186 1.00 42.06 C ATOM 932 CE LYS A 124 71.842 11.023 −43.404 1.00 46.07 C ATOM 933 NZ LYS A 124 73.312 11.366 −43.269 1.00 46.30 N ATOM 934 C LYS A 124 68.989 6.198 −43.984 1.00 45.36 C ATOM 935 O LYS A 124 69.693 5.235 −43.663 1.00 45.33 O ATOM 936 N ALA A 125 68.274 6.214 −45.110 1.00 46.08 N ATOM 937 CA ALA A 125 68.489 5.175 −46.141 1.00 47.11 C ATOM 938 CB ALA A 125 67.648 5.451 −47.384 1.00 46.76 C ATOM 939 C ALA A 125 69.972 5.123 −46.500 1.00 47.33 C ATOM 940 O ALA A 125 70.618 6.175 −46.508 1.00 47.44 O ATOM 941 N ALA A 126 70.528 3.890 −46.738 1.00 48.74 N ATOM 942 CA ALA A 126 71.863 3.817 −47.444 1.00 49.81 C ATOM 943 CB ALA A 126 72.337 2.362 −47.714 1.00 49.59 C ATOM 944 C ALA A 126 71.800 4.577 −48.758 1.00 49.59 C ATOM 945 O ALA A 126 70.772 4.531 −49.478 1.00 51.31 O ATOM 946 OXT ALA A 126 72.764 5.235 −49.161 1.00 51.16 O ATOM 947 N ALA B 1 32.574 −25.808 −7.345 1.00 54.95 N ATOM 948 CA ALA B 1 31.899 −24.453 −7.214 1.00 54.95 C ATOM 949 CB ALA B 1 32.851 −23.438 −6.634 1.00 55.01 C ATOM 950 C ALA B 1 31.283 −23.899 −8.498 1.00 54.51 C ATOM 951 O ALA B 1 31.993 −23.349 −9.338 1.00 55.95 O ATOM 952 N TRP B 2 29.963 −23.999 −8.630 1.00 53.08 N ATOM 953 CA TRP B 2 29.268 −23.472 −9.820 1.00 50.94 C ATOM 954 CB TRP B 2 29.049 −24.605 −10.808 1.00 51.28 C ATOM 955 CG TRP B 2 28.244 −25.758 −10.275 1.00 51.82 C ATOM 956 CD1 TRP B 2 28.645 −26.700 −9.352 1.00 52.56 C ATOM 957 NE1 TRP B 2 27.625 −27.612 −9.141 1.00 53.31 N ATOM 958 CE2 TRP B 2 26.550 −27.281 −9.932 1.00 51.80 C ATOM 959 CD2 TRP B 2 26.903 −26.123 −10.670 1.00 51.84 C ATOM 960 CE3 TRP B 2 25.970 −25.573 −11.562 1.00 51.22 C ATOM 961 CZ3 TRP B 2 24.719 −26.207 −11.705 1.00 52.11 C ATOM 962 CH2 TRP B 2 24.404 −27.365 −10.954 1.00 52.45 C ATOM 963 CZ2 TRP B 2 25.303 −27.907 −10.064 1.00 51.92 C ATOM 964 C TRP B 2 27.938 −22.763 −9.508 1.00 49.34 C ATOM 965 O TRP B 2 27.440 −22.864 −8.388 1.00 48.53 O ATOM 966 N VAL B 3 27.368 −22.056 −10.497 1.00 47.43 N ATOM 967 CA VAL B 3 26.076 −21.354 −10.319 1.00 45.64 C ATOM 968 CB VAL B 3 26.099 −19.865 −10.731 1.00 45.32 C ATOM 969 CG1 VAL B 3 24.721 −19.227 −10.539 1.00 42.93 C ATOM 970 CG2 VAL B 3 27.168 −19.097 −9.887 1.00 45.26 C ATOM 971 C VAL B 3 24.945 −22.081 −11.021 1.00 45.65 C ATOM 972 O VAL B 3 24.996 −22.334 −12.239 1.00 45.33 O ATOM 973 N ASP B 4 23.951 −22.435 −10.211 1.00 44.65 N ATOM 974 CA ASP B 4 22.792 −23.198 −10.608 1.00 44.39 C ATOM 975 CB ASP B 4 22.440 −24.131 −9.458 1.00 44.31 C ATOM 976 CG ASP B 4 21.422 −25.186 −9.834 1.00 48.07 C ATOM 977 OD1 ASP B 4 20.972 −25.212 −11.005 1.00 48.90 O ATOM 978 OD2 ASP B 4 21.052 −25.997 −8.932 1.00 51.27 O ATOM 979 C ASP B 4 21.621 −22.242 −10.868 1.00 44.17 C ATOM 980 O ASP B 4 20.926 −21.829 −9.913 1.00 45.13 O ATOM 981 N GLN B 5 21.411 −21.881 −12.140 1.00 41.99 N ATOM 982 CA GLN B 5 20.330 −20.945 −12.536 1.00 40.63 C ATOM 983 CB GLN B 5 20.776 −20.017 −13.679 1.00 38.50 C ATOM 984 CG GLN B 5 19.743 −18.908 −14.001 1.00 38.32 C ATOM 985 CD GLN B 5 20.265 −17.971 −15.026 1.00 40.18 C ATOM 986 OE1 GLN B 5 21.484 −17.928 −15.203 1.00 40.72 O ATOM 987 NE2 GLN B 5 19.367 −17.207 −15.738 1.00 32.03 N ATOM 988 C GLN B 5 19.078 −21.717 −12.978 1.00 40.31 C ATOM 989 O GLN B 5 19.183 −22.575 −13.867 1.00 40.15 O ATOM 990 N THR B 6 17.928 −21.407 −12.360 1.00 40.19 N ATOM 991 CA THR B 6 16.597 −21.960 −12.747 1.00 41.32 C ATOM 992 CB THR B 6 16.104 −23.106 −11.802 1.00 42.19 C ATOM 993 OG1 THR B 6 16.242 −22.695 −10.438 1.00 45.35 O ATOM 994 CG2 THR B 6 16.930 −24.421 −11.980 1.00 42.80 C ATOM 995 C THR B 6 15.521 −20.844 −12.901 1.00 40.56 C ATOM 996 O THR B 6 15.543 −19.855 −12.194 1.00 41.21 O ATOM 997 N PRO B 7 14.605 −20.982 −13.859 1.00 40.24 N ATOM 998 CA PRO B 7 14.476 −22.120 −14.793 1.00 39.70 C ATOM 999 CB PRO B 7 13.018 −22.018 −15.237 1.00 38.51 C ATOM 1000 CG PRO B 7 12.763 −20.573 −15.267 1.00 37.58 C ATOM 1001 CD PRO B 7 13.570 −19.975 −14.102 1.00 39.88 C ATOM 1002 C PRO B 7 15.428 −21.915 −15.952 1.00 39.21 C ATOM 1003 O PRO B 7 15.772 −20.760 −16.237 1.00 40.93 O ATOM 1004 N ARG B 8 15.863 −22.985 −16.598 1.00 39.22 N ATOM 1005 CA ARG B 8 16.691 −22.864 −17.793 1.00 41.90 C ATOM 1006 CB ARG B 8 17.582 −24.141 −17.979 1.00 40.92 C ATOM 1007 CG ARG B 8 19.021 −23.843 −17.244 1.00 46.48 C ATOM 1008 CD ARG B 8 20.003 −25.051 −17.078 1.00 49.30 C ATOM 1009 NE ARG B 8 20.903 −25.344 −18.231 1.00 58.14 N ATOM 1010 CZ ARG B 8 21.129 −24.550 −19.298 1.00 60.29 C ATOM 1011 NH1 ARG B 8 21.970 −24.991 −20.239 1.00 62.88 N ATOM 1012 NH2 ARG B 8 20.541 −23.343 −19.446 1.00 55.02 N ATOM 1013 C ARG B 8 15.916 −22.266 −19.062 1.00 41.20 C ATOM 1014 O ARG B 8 16.488 −21.531 −19.915 1.00 39.59 O ATOM 1015 N THR B 9 14.594 −22.472 −19.057 1.00 40.29 N ATOM 1016 CA THR B 9 13.687 −22.185 −20.154 1.00 41.50 C ATOM 1017 CB THR B 9 13.369 −23.496 −20.870 1.00 41.08 C ATOM 1018 OG1 THR B 9 14.478 −23.831 −21.716 1.00 44.54 O ATOM 1019 CG2 THR B 9 12.186 −23.397 −21.691 1.00 44.46 C ATOM 1020 C THR B 9 12.420 −21.625 −19.532 1.00 41.17 C ATOM 1021 O THR B 9 11.988 −22.105 −18.486 1.00 42.29 O ATOM 1022 N ALA B 10 11.863 −20.577 −20.120 1.00 39.83 N ATOM 1023 CA ALA B 10 10.527 −20.109 −19.709 1.00 39.81 C ATOM 1024 CB ALA B 10 10.636 −19.150 −18.520 1.00 39.10 C ATOM 1025 C ALA B 10 9.708 −19.486 −20.865 1.00 39.00 C ATOM 1026 O ALA B 10 10.218 −18.783 −21.709 1.00 37.05 O ATOM 1027 N THR B 11 8.433 −19.807 −20.926 1.00 41.44 N ATOM 1028 CA THR B 11 7.504 −19.035 −21.763 1.00 42.21 C ATOM 1029 CB THR B 11 7.116 −19.744 −23.092 1.00 43.19 C ATOM 1030 OG1 THR B 11 5.708 −19.620 −23.359 1.00 45.57 O ATOM 1031 CG2 THR B 11 7.568 −21.172 −23.089 1.00 43.44 C ATOM 1032 C THR B 11 6.410 −18.391 −20.904 1.00 43.25 C ATOM 1033 O THR B 11 5.846 −19.026 −20.001 1.00 42.68 O ATOM 1034 N LYS B 12 6.255 −17.074 −21.067 1.00 43.20 N ATOM 1035 CA LYS B 12 5.257 −16.353 −20.305 1.00 43.24 C ATOM 1036 CB LYS B 12 5.922 −15.425 −19.313 1.00 43.55 C ATOM 1037 CG LYS B 12 6.850 −16.125 −18.282 1.00 43.71 C ATOM 1038 CD LYS B 12 6.045 −16.918 −17.255 1.00 46.08 C ATOM 1039 CE LYS B 12 6.956 −17.432 −16.177 1.00 46.77 C ATOM 1040 NZ LYS B 12 6.207 −18.212 −15.178 1.00 48.14 N ATOM 1041 C LYS B 12 4.323 −15.587 −21.224 1.00 43.67 C ATOM 1042 O LYS B 12 4.603 −15.377 −22.399 1.00 43.55 O ATOM 1043 N GLU B 13 3.196 −15.198 −20.670 1.00 44.88 N ATOM 1044 CA GLU B 13 2.183 −14.407 −21.349 1.00 45.97 C ATOM 1045 CB GLU B 13 0.819 −14.763 −20.763 1.00 45.50 C ATOM 1046 CG GLU B 13 −0.252 −14.954 −21.805 1.00 51.14 C ATOM 1047 CD GLU B 13 −1.672 −15.025 −21.223 1.00 52.49 C ATOM 1048 OE1 GLU B 13 −2.214 −13.977 −20.736 1.00 56.84 O ATOM 1049 OE2 GLU B 13 −2.268 −16.136 −21.318 1.00 61.96 O ATOM 1050 C GLU B 13 2.512 −12.959 −21.020 1.00 43.04 C ATOM 1051 O GLU B 13 3.028 −12.701 −19.945 1.00 41.31 O ATOM 1052 N THR B 14 2.223 −12.015 −21.916 1.00 41.79 N ATOM 1053 CA THR B 14 2.424 −10.600 −21.549 1.00 41.84 C ATOM 1054 CB THR B 14 2.091 −9.590 −22.653 1.00 41.46 C ATOM 1055 OG1 THR B 14 0.695 −9.668 −22.914 1.00 46.96 O ATOM 1056 CG2 THR B 14 2.850 −9.885 −23.954 1.00 39.14 C ATOM 1057 C THR B 14 1.601 −10.261 −20.284 1.00 41.06 C ATOM 1058 O THR B 14 0.519 −10.798 −20.082 1.00 39.53 O ATOM 1059 N GLY B 15 2.167 −9.424 −19.419 1.00 39.95 N ATOM 1060 CA GLY B 15 1.531 −9.033 −18.178 1.00 39.59 C ATOM 1061 C GLY B 15 1.928 −9.927 −17.032 1.00 39.94 C ATOM 1062 O GLY B 15 1.745 −9.553 −15.861 1.00 40.01 O ATOM 1063 N GLU B 16 2.448 −11.112 −17.347 1.00 40.07 N ATOM 1064 CA GLU B 16 2.963 −12.013 −16.311 1.00 41.17 C ATOM 1065 CB GLU B 16 3.024 −13.455 −16.850 1.00 40.57 C ATOM 1066 CG GLU B 16 1.656 −14.146 −16.761 1.00 41.94 C ATOM 1067 CD GLU B 16 1.562 −15.517 −17.442 1.00 43.73 C ATOM 1068 OE1 GLU B 16 2.530 −16.134 −17.948 1.00 43.61 O ATOM 1069 OE2 GLU B 16 0.432 −16.009 −17.477 1.00 54.01 O ATOM 1070 C GLU B 16 4.321 −11.577 −15.715 1.00 40.58 C ATOM 1071 O GLU B 16 4.936 −10.595 −16.140 1.00 41.16 O ATOM 1072 N SER B 17 4.803 −12.311 −14.732 1.00 40.31 N ATOM 1073 CA SER B 17 6.133 −12.054 −14.205 1.00 39.94 C ATOM 1074 CB SER B 17 5.987 −11.519 −12.797 1.00 40.72 C ATOM 1075 OG SER B 17 5.762 −12.588 −11.942 1.00 41.64 O ATOM 1076 C SER B 17 7.004 −13.346 −14.277 1.00 39.37 C ATOM 1077 O SER B 17 6.488 −14.426 −14.552 1.00 39.99 O ATOM 1078 N LEU B 18 8.320 −13.220 −14.120 1.00 39.17 N ATOM 1079 CA LEU B 18 9.270 −14.346 −14.176 1.00 39.40 C ATOM 1080 CB LEU B 18 10.217 −14.269 −15.412 1.00 39.88 C ATOM 1081 CG LEU B 18 10.975 −15.464 −16.093 1.00 39.25 C ATOM 1082 CD1 LEU B 18 12.361 −15.081 −16.621 1.00 36.41 C ATOM 1083 CD2 LEU B 18 11.031 −16.801 −15.375 1.00 36.79 C ATOM 1084 C LEU B 18 10.151 −14.217 −12.952 1.00 39.21 C ATOM 1085 O LEU B 18 10.648 −13.131 −12.684 1.00 38.56 O ATOM 1086 N THR B 19 10.350 −15.309 −12.208 1.00 39.51 N ATOM 1087 CA THR B 19 11.356 −15.331 −11.145 1.00 38.61 C ATOM 1088 CB THR B 19 10.745 −15.681 −9.777 1.00 39.40 C ATOM 1089 OG1 THR B 19 9.596 −14.859 −9.569 1.00 40.21 O ATOM 1090 CG2 THR B 19 11.734 −15.391 −8.613 1.00 37.97 C ATOM 1091 C THR B 19 12.481 −16.291 −11.544 1.00 39.08 C ATOM 1092 O THR B 19 12.242 −17.425 −11.918 1.00 38.36 O ATOM 1093 N ILE B 20 13.713 −15.795 −11.510 1.00 39.84 N ATOM 1094 CA ILE B 20 14.881 −16.577 −11.832 1.00 40.37 C ATOM 1095 CB ILE B 20 15.752 −15.886 −12.869 1.00 41.04 C ATOM 1096 CG1 ILE B 20 14.963 −15.656 −14.189 1.00 41.04 C ATOM 1097 CD1 ILE B 20 15.801 −14.744 −15.167 1.00 40.82 C ATOM 1098 CG2 ILE B 20 17.039 −16.690 −13.157 1.00 37.32 C ATOM 1099 C ILE B 20 15.653 −16.721 −10.544 1.00 42.32 C ATOM 1100 O ILE B 20 15.910 −15.743 −9.821 1.00 42.02 O ATOM 1101 N ASN B 21 16.009 −17.959 −10.235 1.00 43.42 N ATOM 1102 CA ASN B 21 16.750 −18.232 −9.028 1.00 44.99 C ATOM 1103 CB ASN B 21 15.975 −19.274 −8.234 1.00 45.42 C ATOM 1104 CG ASN B 21 14.760 −18.676 −7.544 1.00 49.78 C ATOM 1105 OD1 ASN B 21 14.911 −17.898 −6.575 1.00 55.43 O ATOM 1106 ND2 ASN B 21 13.546 −19.031 −8.021 1.00 48.66 N ATOM 1107 C ASN B 21 18.162 −18.714 −9.316 1.00 45.15 C ATOM 1108 O ASN B 21 18.355 −19.604 −10.139 1.00 46.04 O ATOM 1109 N CYS B 22 19.145 −18.141 −8.642 1.00 45.51 N ATOM 1110 CA CYS B 22 20.512 −18.645 −8.738 1.00 46.56 C ATOM 1111 CB CYS B 22 21.398 −17.616 −9.407 1.00 46.01 C ATOM 1112 SG CYS B 22 20.937 −17.240 −11.134 1.00 54.66 S ATOM 1113 C CYS B 22 21.094 −19.006 −7.382 1.00 46.14 C ATOM 1114 O CYS B 22 20.802 −18.342 −6.400 1.00 45.68 O ATOM 1115 N VAL B 23 21.914 −20.064 −7.348 1.00 46.34 N ATOM 1116 CA VAL B 23 22.574 −20.552 −6.137 1.00 45.67 C ATOM 1117 CB VAL B 23 21.951 −21.906 −5.581 1.00 45.26 C ATOM 1118 CG1 VAL B 23 22.335 −22.151 −4.112 1.00 44.69 C ATOM 1119 CG2 VAL B 23 20.461 −21.936 −5.697 1.00 46.49 C ATOM 1120 C VAL B 23 24.018 −20.856 −6.513 1.00 46.67 C ATOM 1121 O VAL B 23 24.255 −21.594 −7.477 1.00 46.49 O ATOM 1122 N LEU B 24 24.964 −20.275 −5.775 1.00 47.05 N ATOM 1123 CA LEU B 24 26.379 −20.661 −5.783 1.00 49.11 C ATOM 1124 CB LEU B 24 27.194 −19.589 −5.042 1.00 48.19 C ATOM 1125 CG LEU B 24 28.539 −19.018 −5.483 1.00 50.04 C ATOM 1126 CD1 LEU B 24 29.178 −18.189 −4.317 1.00 47.71 C ATOM 1127 CD2 LEU B 24 29.500 −20.085 −5.957 1.00 51.22 C ATOM 1128 C LEU B 24 26.508 −21.967 −4.994 1.00 50.50 C ATOM 1129 O LEU B 24 26.243 −21.987 −3.785 1.00 50.47 O ATOM 1130 N ARG B 25 26.902 −23.047 −5.670 1.00 52.28 N ATOM 1131 CA ARG B 25 27.026 −24.372 −5.044 1.00 53.42 C ATOM 1132 CB ARG B 25 26.429 −25.461 −5.933 1.00 53.07 C ATOM 1133 CG ARG B 25 25.046 −25.141 −6.419 1.00 51.09 C ATOM 1134 CD ARG B 25 24.139 −26.318 −6.287 1.00 51.67 C ATOM 1135 NE ARG B 25 22.742 −25.901 −6.377 1.00 52.28 N ATOM 1136 CZ ARG B 25 21.895 −25.907 −5.354 1.00 51.59 C ATOM 1137 NH1 ARG B 25 22.299 −26.334 −4.157 1.00 51.61 N ATOM 1138 NH2 ARG B 25 20.644 −25.498 −5.532 1.00 50.56 N ATOM 1139 C ARG B 25 28.483 −24.685 −4.733 1.00 55.51 C ATOM 1140 O ARG B 25 29.364 −23.827 −4.909 1.00 55.95 O ATOM 1141 N ASP B 26 28.724 −25.902 −4.238 1.00 57.67 N ATOM 1142 CA ASP B 26 30.064 −26.414 −3.891 1.00 59.47 C ATOM 1143 CB ASP B 26 30.592 −27.321 −5.009 1.00 59.83 C ATOM 1144 CG ASP B 26 29.669 −28.511 −5.285 1.00 61.62 C ATOM 1145 OD1 ASP B 26 28.795 −28.416 −6.198 1.00 62.14 O ATOM 1146 OD2 ASP B 26 29.814 −29.530 −4.572 1.00 62.86 O ATOM 1147 C ASP B 26 31.052 −25.293 −3.599 1.00 60.27 C ATOM 1148 O ASP B 26 32.103 −25.207 −4.225 1.00 60.76 O ATOM 1149 N ALA B 27 30.693 −24.433 −2.646 1.00 61.28 N ATOM 1150 CA ALA B 27 31.493 −23.273 −2.307 1.00 61.93 C ATOM 1151 CB ALA B 27 30.784 −22.014 −2.708 1.00 61.89 C ATOM 1152 C ALA B 27 31.863 −23.212 −0.829 1.00 62.84 C ATOM 1153 O ALA B 27 30.991 −23.186 0.053 1.00 63.36 O ATOM 1154 N SER B 28 33.171 −23.214 −0.581 1.00 63.10 N ATOM 1155 CA SER B 28 33.737 −22.641 0.624 1.00 63.63 C ATOM 1156 CB SER B 28 35.224 −22.968 0.718 1.00 63.90 C ATOM 1157 OG SER B 28 35.570 −24.105 −0.058 1.00 64.95 O ATOM 1158 C SER B 28 33.601 −21.129 0.427 1.00 63.77 C ATOM 1159 O SER B 28 33.495 −20.363 1.393 1.00 64.47 O ATOM 1160 N PHE B 29 33.625 −20.737 −0.852 1.00 63.20 N ATOM 1161 CA PHE B 29 33.530 −19.355 −1.334 1.00 62.45 C ATOM 1162 CB PHE B 29 33.358 −19.335 −2.872 1.00 62.20 C ATOM 1163 CG PHE B 29 34.395 −20.140 −3.656 1.00 60.55 C ATOM 1164 CD1 PHE B 29 35.699 −20.308 −3.201 1.00 60.68 C ATOM 1165 CE1 PHE B 29 36.646 −21.025 −3.950 1.00 60.56 C ATOM 1166 CZ PHE B 29 36.304 −21.564 −5.173 1.00 60.35 C ATOM 1167 CE2 PHE B 29 35.014 −21.392 −5.648 1.00 62.60 C ATOM 1168 CD2 PHE B 29 34.066 −20.671 −4.891 1.00 61.14 C ATOM 1169 C PHE B 29 32.352 −18.604 −0.706 1.00 62.55 C ATOM 1170 O PHE B 29 31.268 −19.188 −0.504 1.00 62.53 O ATOM 1171 N GLU B 30 32.545 −17.315 −0.411 1.00 61.80 N ATOM 1172 CA GLU B 30 31.445 −16.518 0.143 1.00 61.37 C ATOM 1173 CB GLU B 30 31.797 −15.884 1.497 1.00 61.71 C ATOM 1174 CG GLU B 30 32.680 −14.633 1.411 1.00 64.15 C ATOM 1175 CD GLU B 30 32.153 −13.451 2.233 1.00 65.74 C ATOM 1176 OE1 GLU B 30 32.866 −13.015 3.168 1.00 63.81 O ATOM 1177 OE2 GLU B 30 31.033 −12.963 1.925 1.00 66.59 O ATOM 1178 C GLU B 30 30.920 −15.470 −0.836 1.00 59.86 C ATOM 1179 O GLU B 30 31.681 −14.655 −1.343 1.00 59.82 O ATOM 1180 N LEU B 31 29.606 −15.497 −1.069 1.00 58.15 N ATOM 1181 CA LEU B 31 28.946 −14.572 −1.982 1.00 56.44 C ATOM 1182 CB LEU B 31 27.444 −14.831 −1.998 1.00 56.25 C ATOM 1183 CG LEU B 31 26.669 −14.204 −3.148 1.00 54.16 C ATOM 1184 CD1 LEU B 31 27.090 −14.868 −4.401 1.00 51.33 C ATOM 1185 CD2 LEU B 31 25.183 −14.389 −2.910 1.00 53.29 C ATOM 1186 C LEU B 31 29.187 −13.136 −1.575 1.00 55.70 C ATOM 1187 O LEU B 31 28.791 −12.748 −0.489 1.00 55.50 O ATOM 1188 N LYS B 32 29.831 −12.354 −2.436 1.00 54.55 N ATOM 1189 CA LYS B 32 30.081 −10.963 −2.096 1.00 54.28 C ATOM 1190 CB LYS B 32 31.576 −10.589 −2.202 1.00 54.33 C ATOM 1191 CG LYS B 32 31.918 −9.629 −3.367 1.00 56.46 C ATOM 1192 CD LYS B 32 33.271 −8.944 −3.278 1.00 55.97 C ATOM 1193 CE LYS B 32 33.233 −7.762 −2.288 1.00 63.91 C ATOM 1194 NZ LYS B 32 32.451 −6.536 −2.708 1.00 64.90 N ATOM 1195 C LYS B 32 29.216 −10.009 −2.902 1.00 52.81 C ATOM 1196 O LYS B 32 28.927 −8.898 −2.450 1.00 52.61 O ATOM 1197 N ASP B 33 28.818 −10.438 −4.093 1.00 51.52 N ATOM 1198 CA ASP B 33 28.077 −9.585 −5.000 1.00 50.34 C ATOM 1199 CB ASP B 33 29.020 −8.581 −5.653 1.00 51.45 C ATOM 1200 CG ASP B 33 28.458 −7.192 −5.654 1.00 54.79 C ATOM 1201 OD1 ASP B 33 29.150 −6.290 −5.130 1.00 60.70 O ATOM 1202 OD2 ASP B 33 27.308 −6.997 −6.126 1.00 60.01 O ATOM 1203 C ASP B 33 27.349 −10.349 −6.103 1.00 48.37 C ATOM 1204 O ASP B 33 27.618 −11.514 −6.338 1.00 47.51 O ATOM 1205 N THR B 34 26.435 −9.656 −6.783 1.00 46.63 N ATOM 1206 CA THR B 34 25.607 −10.230 −7.812 1.00 45.52 C ATOM 1207 CB THR B 34 24.228 −10.594 −7.311 1.00 45.26 C ATOM 1208 OG1 THR B 34 23.507 −9.400 −7.005 1.00 44.94 O ATOM 1209 CG2 THR B 34 24.280 −11.520 −6.066 1.00 46.07 C ATOM 1210 C THR B 34 25.396 −9.238 −8.924 1.00 45.83 C ATOM 1211 O THR B 34 25.372 −8.017 −8.702 1.00 45.11 O ATOM 1212 N GLY B 35 25.201 −9.773 −10.125 1.00 45.83 N ATOM 1213 CA GLY B 35 24.725 −8.972 −11.249 1.00 44.82 C ATOM 1214 C GLY B 35 23.816 −9.785 −12.153 1.00 43.28 C ATOM 1215 O GLY B 35 23.801 −11.019 −12.111 1.00 42.32 O ATOM 1216 N TRP B 36 23.074 −9.070 −12.992 1.00 42.69 N ATOM 1217 CA TRP B 36 22.094 −9.665 −13.876 1.00 42.22 C ATOM 1218 CB TRP B 36 20.695 −9.393 −13.321 1.00 41.99 C ATOM 1219 CG TRP B 36 20.426 −10.204 −12.070 1.00 42.02 C ATOM 1220 CD1 TRP B 36 20.606 −9.809 −10.785 1.00 39.92 C ATOM 1221 NE1 TRP B 36 20.263 −10.839 −9.929 1.00 42.86 N ATOM 1222 CE2 TRP B 36 19.869 −11.931 −10.660 1.00 41.27 C ATOM 1223 CD2 TRP B 36 19.955 −11.571 −12.021 1.00 41.39 C ATOM 1224 CE3 TRP B 36 19.601 −12.520 −13.014 1.00 42.24 C ATOM 1225 CZ3 TRP B 36 19.161 −13.779 −12.616 1.00 42.06 C ATOM 1226 CH2 TRP B 36 19.077 −14.117 −11.226 1.00 42.99 C ATOM 1227 CZ2 TRP B 36 19.428 −13.199 −10.235 1.00 42.30 C ATOM 1228 C TRP B 36 22.263 −9.062 −15.251 1.00 42.47 C ATOM 1229 O TRP B 36 22.527 −7.848 −15.372 1.00 43.87 O ATOM 1230 N TYR B 37 22.124 −9.884 −16.284 1.00 42.85 N ATOM 1231 CA TYR B 37 22.396 −9.464 −17.688 1.00 44.60 C ATOM 1232 CB TYR B 37 23.771 −9.983 −18.167 1.00 45.76 C ATOM 1233 CG TYR B 37 24.857 −9.689 −17.146 1.00 47.71 C ATOM 1234 CD1 TYR B 37 25.524 −8.464 −17.117 1.00 50.27 C ATOM 1235 CE1 TYR B 37 26.524 −8.179 −16.125 1.00 51.99 C ATOM 1236 CZ TYR B 37 26.825 −9.195 −15.183 1.00 53.06 C ATOM 1237 OH TYR B 37 27.770 −9.042 −14.172 1.00 54.16 O ATOM 1238 CE2 TYR B 37 26.137 −10.395 −15.213 1.00 54.10 C ATOM 1239 CD2 TYR B 37 25.163 −10.627 −16.175 1.00 51.46 C ATOM 1240 C TYR B 37 21.332 −10.026 −18.555 1.00 44.88 C ATOM 1241 O TYR B 37 20.705 −11.043 −18.209 1.00 45.77 O ATOM 1242 N ARG B 38 21.135 −9.388 −19.698 1.00 45.01 N ATOM 1243 CA ARG B 38 20.136 −9.799 −20.689 1.00 44.85 C ATOM 1244 CB ARG B 38 18.859 −8.971 −20.449 1.00 44.48 C ATOM 1245 CG ARG B 38 17.818 −8.990 −21.512 1.00 49.57 C ATOM 1246 CD ARG B 38 16.572 −8.154 −21.096 1.00 50.80 C ATOM 1247 NE ARG B 38 16.808 −6.728 −20.931 1.00 59.29 N ATOM 1248 CZ ARG B 38 16.791 −5.849 −21.929 1.00 65.43 C ATOM 1249 NH1 ARG B 38 16.570 −6.250 −23.196 1.00 68.18 N ATOM 1250 NH2 ARG B 38 17.020 −4.560 −21.670 1.00 66.70 N ATOM 1251 C ARG B 38 20.678 −9.588 −22.100 1.00 43.70 C ATOM 1252 O ARG B 38 21.291 −8.573 −22.413 1.00 43.08 O ATOM 1253 N THR B 39 20.399 −10.551 −22.970 1.00 43.10 N ATOM 1254 CA THR B 39 20.574 −10.401 −24.392 1.00 41.41 C ATOM 1255 CB THR B 39 21.561 −11.463 −24.921 1.00 40.29 C ATOM 1256 OG1 THR B 39 22.780 −11.325 −24.192 1.00 44.60 O ATOM 1257 CG2 THR B 39 21.830 −11.278 −26.361 1.00 38.65 C ATOM 1258 C THR B 39 19.209 −10.611 −25.023 1.00 40.66 C ATOM 1259 O THR B 39 18.632 −11.718 −24.960 1.00 40.48 O ATOM 1260 N LYS B 40 18.696 −9.575 −25.658 1.00 38.27 N ATOM 1261 CA LYS B 40 17.420 −9.673 −26.286 1.00 40.05 C ATOM 1262 CB LYS B 40 16.985 −8.329 −26.866 1.00 40.66 C ATOM 1263 CG LYS B 40 18.180 −7.401 −27.336 1.00 46.79 C ATOM 1264 CD LYS B 40 19.495 −7.235 −26.337 1.00 45.68 C ATOM 1265 CE LYS B 40 20.177 −5.941 −26.663 1.00 47.93 C ATOM 1266 NZ LYS B 40 19.625 −5.348 −28.020 1.00 50.16 N ATOM 1267 C LYS B 40 17.399 −10.781 −27.346 1.00 39.05 C ATOM 1268 O LYS B 40 18.428 −11.090 −27.963 1.00 38.47 O ATOM 1269 N LEU B 41 16.231 −11.387 −27.526 1.00 37.38 N ATOM 1270 CA LEU B 41 16.110 −12.482 −28.447 1.00 36.97 C ATOM 1271 CB LEU B 41 14.693 −13.025 −28.410 1.00 35.93 C ATOM 1272 CG LEU B 41 14.361 −14.498 −28.751 1.00 38.03 C ATOM 1273 CD1 LEU B 41 15.260 −15.201 −29.688 1.00 29.12 C ATOM 1274 CD2 LEU B 41 12.935 −14.628 −29.245 1.00 34.95 C ATOM 1275 C LEU B 41 16.456 −12.015 −29.853 1.00 37.90 C ATOM 1276 O LEU B 41 15.750 −11.171 −30.429 1.00 38.11 O ATOM 1277 N GLY B 42 17.516 −12.596 −30.428 1.00 38.84 N ATOM 1278 CA GLY B 42 17.894 −12.309 −31.828 1.00 39.84 C ATOM 1279 C GLY B 42 19.138 −11.426 −31.882 1.00 41.12 C ATOM 1280 O GLY B 42 19.889 −11.451 −32.845 1.00 40.47 O ATOM 1281 N SER B 43 19.398 −10.703 −30.795 1.00 42.54 N ATOM 1282 CA SER B 43 20.505 −9.752 −30.700 1.00 43.80 C ATOM 1283 CB SER B 43 20.102 −8.627 −29.733 1.00 43.55 C ATOM 1284 OG SER B 43 21.263 −8.058 −29.131 1.00 47.40 O ATOM 1285 C SER B 43 21.837 −10.389 −30.246 1.00 44.08 C ATOM 1286 O SER B 43 21.850 −11.442 −29.639 1.00 43.11 O ATOM 1287 N THR B 44 22.950 −9.730 −30.556 1.00 46.01 N ATOM 1288 CA THR B 44 24.284 −10.132 −30.088 1.00 49.08 C ATOM 1289 CB THR B 44 25.386 −9.746 −31.113 1.00 49.56 C ATOM 1290 OG1 THR B 44 24.825 −8.862 −32.111 1.00 50.26 O ATOM 1291 CG2 THR B 44 25.951 −10.982 −31.782 1.00 51.25 C ATOM 1292 C THR B 44 24.609 −9.414 −28.788 1.00 50.25 C ATOM 1293 O THR B 44 25.441 −9.865 −27.991 1.00 51.27 O ATOM 1294 N ASN B 45 23.915 −8.304 −28.560 1.00 51.11 N ATOM 1295 CA ASN B 45 24.288 −7.373 −27.522 1.00 51.61 C ATOM 1296 CB ASN B 45 23.900 −5.973 −27.975 1.00 51.54 C ATOM 1297 CG ASN B 45 24.666 −5.532 −29.257 1.00 52.45 C ATOM 1298 OD1 ASN B 45 24.146 −4.760 −30.070 1.00 52.60 O ATOM 1299 ND2 ASN B 45 25.895 −6.033 −29.433 1.00 53.59 N ATOM 1300 C ASN B 45 23.809 −7.699 −26.105 1.00 51.58 C ATOM 1301 O ASN B 45 22.632 −7.837 −25.840 1.00 52.48 O ATOM 1302 N GLU B 46 24.750 −7.844 −25.189 1.00 51.92 N ATOM 1303 CA GLU B 46 24.414 −8.133 −23.821 1.00 52.44 C ATOM 1304 CB GLU B 46 25.368 −9.161 −23.221 1.00 52.91 C ATOM 1305 CG GLU B 46 24.884 −9.678 −21.894 1.00 58.15 C ATOM 1306 CD GLU B 46 25.957 −10.405 −21.123 1.00 66.36 C ATOM 1307 OE1 GLU B 46 25.706 −11.582 −20.727 1.00 70.62 O ATOM 1308 OE2 GLU B 46 27.039 −9.793 −20.894 1.00 69.30 O ATOM 1309 C GLU B 46 24.380 −6.860 −22.976 1.00 51.53 C ATOM 1310 O GLU B 46 25.327 −6.088 −22.964 1.00 53.42 O ATOM 1311 N GLN B 47 23.278 −6.642 −22.286 1.00 49.40 N ATOM 1312 CA GLN B 47 23.107 −5.475 −21.450 1.00 48.39 C ATOM 1313 CB GLN B 47 21.867 −4.713 −21.877 1.00 48.97 C ATOM 1314 CG GLN B 47 21.851 −4.315 −23.390 1.00 54.17 C ATOM 1315 CD GLN B 47 22.859 −3.187 −23.733 1.00 58.95 C ATOM 1316 OE1 GLN B 47 22.457 −2.123 −24.216 1.00 59.67 O ATOM 1317 NE2 GLN B 47 24.167 −3.430 −23.488 1.00 56.36 N ATOM 1318 C GLN B 47 22.954 −5.913 −20.012 1.00 46.93 C ATOM 1319 O GLN B 47 22.368 −6.955 −19.731 1.00 45.54 O ATOM 1320 N SER B 48 23.510 −5.138 −19.103 1.00 45.48 N ATOM 1321 CA SER B 48 23.310 −5.430 −17.703 1.00 45.97 C ATOM 1322 CB SER B 48 24.518 −5.024 −16.823 1.00 44.83 C ATOM 1323 OG SER B 48 24.567 −3.634 −16.677 1.00 48.28 O ATOM 1324 C SER B 48 21.996 −4.775 −17.260 1.00 45.25 C ATOM 1325 O SER B 48 21.625 −3.706 −17.747 1.00 44.79 O ATOM 1326 N ILE B 49 21.310 −5.440 −16.336 1.00 44.46 N ATOM 1327 CA ILE B 49 19.994 −5.034 −15.879 1.00 43.57 C ATOM 1328 CB ILE B 49 19.191 −6.343 −15.528 1.00 43.55 C ATOM 1329 CG1 ILE B 49 18.786 −7.071 −16.799 1.00 41.77 C ATOM 1330 CD1 ILE B 49 18.315 −8.465 −16.522 1.00 45.18 C ATOM 1331 CG2 ILE B 49 17.998 −6.077 −14.627 1.00 42.15 C ATOM 1332 C ILE B 49 20.202 −4.130 −14.678 1.00 43.36 C ATOM 1333 O ILE B 49 20.937 −4.516 −13.800 1.00 43.25 O ATOM 1334 N SER B 50 19.619 −2.910 −14.657 1.00 44.45 N ATOM 1335 CA SER B 50 19.533 −2.085 −13.399 1.00 44.63 C ATOM 1336 CB SER B 50 19.444 −0.561 −13.621 1.00 44.94 C ATOM 1337 OG SER B 50 19.832 −0.190 −14.927 1.00 49.21 O ATOM 1338 C SER B 50 18.328 −2.500 −12.603 1.00 43.86 C ATOM 1339 O SER B 50 17.189 −2.461 −13.099 1.00 43.03 O ATOM 1340 N ILE B 51 18.603 −2.881 −11.369 1.00 43.39 N ATOM 1341 CA ILE B 51 17.624 −3.379 −10.447 1.00 43.30 C ATOM 1342 CB ILE B 51 18.340 −3.979 −9.224 1.00 43.57 C ATOM 1343 CG1 ILE B 51 19.287 −5.151 −9.618 1.00 44.05 C ATOM 1344 CD1 ILE B 51 18.667 −6.326 −10.418 1.00 35.96 C ATOM 1345 CG2 ILE B 51 17.357 −4.242 −8.073 1.00 43.78 C ATOM 1346 C ILE B 51 16.771 −2.224 −9.993 1.00 44.13 C ATOM 1347 O ILE B 51 17.287 −1.167 −9.601 1.00 45.28 O ATOM 1348 N GLY B 52 15.456 −2.413 −10.016 1.00 44.21 N ATOM 1349 CA GLY B 52 14.540 −1.395 −9.504 1.00 43.63 C ATOM 1350 C GLY B 52 13.381 −1.293 −10.469 1.00 43.28 C ATOM 1351 O GLY B 52 13.460 −1.784 −11.585 1.00 43.58 O ATOM 1352 N GLY B 53 12.310 −0.656 −10.035 1.00 43.27 N ATOM 1353 CA GLY B 53 11.083 −0.560 −10.850 1.00 42.78 C ATOM 1354 C GLY B 53 10.462 −2.015 −10.752 1.00 43.77 C ATOM 1355 O GLY B 53 9.995 −2.673 −9.640 1.00 43.34 O ATOM 1356 N ARG B 54 10.551 −2.654 −12.075 1.00 43.61 N ATOM 1357 CA ARG B 54 9.886 −3.914 −12.251 1.00 42.86 C ATOM 1358 CB ARG B 54 9.068 −3.913 −13.539 1.00 44.13 C ATOM 1359 CG ARG B 54 9.889 −3.906 −14.830 1.00 42.33 C ATOM 1360 CD ARG B 54 8.906 −3.835 −15.998 1.00 45.56 C ATOM 1361 NE ARG B 54 9.580 −3.821 −17.288 1.00 47.32 N ATOM 1362 CZ ARG B 54 9.650 −4.835 −18.148 1.00 47.04 C ATOM 1363 NH1 ARG B 54 9.064 −6.010 −17.908 1.00 50.81 N ATOM 1364 NH2 ARG B 54 10.306 −4.664 −19.280 1.00 46.49 N ATOM 1365 C ARG B 54 10.892 −5.077 −12.274 1.00 44.33 C ATOM 1366 O ARG B 54 10.498 −6.291 −12.483 1.00 44.77 O ATOM 1367 N TYR B 55 12.186 −4.751 −12.152 1.00 43.57 N ATOM 1368 CA TYR B 55 13.228 −5.749 −11.905 1.00 43.62 C ATOM 1369 CB TYR B 55 14.498 −5.407 −12.673 1.00 44.46 C ATOM 1370 CG TYR B 55 14.287 −5.318 −14.171 1.00 46.09 C ATOM 1371 CD1 TYR B 55 14.032 −4.088 −14.784 1.00 48.85 C ATOM 1372 CE1 TYR B 55 13.812 −3.998 −16.152 1.00 48.27 C ATOM 1373 CZ TYR B 55 13.865 −5.144 −16.918 1.00 48.69 C ATOM 1374 OH TYR B 55 13.655 −5.041 −18.268 1.00 47.96 O ATOM 1375 CE2 TYR B 55 14.087 −6.373 −16.336 1.00 48.31 C ATOM 1376 CD2 TYR B 55 14.296 −6.448 −14.959 1.00 45.72 C ATOM 1377 C TYR B 55 13.511 −5.706 −10.398 1.00 43.55 C ATOM 1378 O TYR B 55 14.064 −4.715 −9.878 1.00 42.28 O ATOM 1379 N VAL B 56 13.071 −6.744 −9.689 1.00 43.19 N ATOM 1380 CA VAL B 56 13.348 −6.837 −8.260 1.00 42.73 C ATOM 1381 CB VAL B 56 12.127 −6.516 −7.293 1.00 42.21 C ATOM 1382 CG1 VAL B 56 10.841 −6.421 −7.968 1.00 44.06 C ATOM 1383 CG2 VAL B 56 12.051 −7.448 −6.048 1.00 45.27 C ATOM 1384 C VAL B 56 14.263 −8.013 −7.898 1.00 42.60 C ATOM 1385 O VAL B 56 13.991 −9.173 −8.224 1.00 41.88 O ATOM 1386 N GLU B 57 15.388 −7.664 −7.277 1.00 42.73 N ATOM 1387 CA GLU B 57 16.395 −8.617 −6.875 1.00 44.06 C ATOM 1388 CB GLU B 57 17.815 −8.148 −7.214 1.00 42.94 C ATOM 1389 CG GLU B 57 18.805 −9.083 −6.512 1.00 44.58 C ATOM 1390 CD GLU B 57 20.228 −9.094 −7.028 1.00 48.71 C ATOM 1391 OE1 GLU B 57 20.904 −8.036 −7.062 1.00 49.40 O ATOM 1392 OE2 GLU B 57 20.704 −10.204 −7.334 1.00 49.94 O ATOM 1393 C GLU B 57 16.271 −8.867 −5.374 1.00 44.37 C ATOM 1394 O GLU B 57 16.096 −7.910 −4.621 1.00 43.80 O ATOM 1395 N THR B 58 16.326 −10.154 −4.985 1.00 45.59 N ATOM 1396 CA THR B 58 16.372 −10.633 −3.584 1.00 47.38 C ATOM 1397 CB THR B 58 15.228 −11.630 −3.244 1.00 47.57 C ATOM 1398 OG1 THR B 58 13.968 −11.157 −3.752 1.00 48.77 O ATOM 1399 CG2 THR B 58 15.109 −11.859 −1.738 1.00 46.75 C ATOM 1400 C THR B 58 17.694 −11.404 −3.420 1.00 48.37 C ATOM 1401 O THR B 58 18.014 −12.246 −4.263 1.00 48.05 O ATOM 1402 N VAL B 59 18.443 −11.121 −2.353 1.00 48.84 N ATOM 1403 CA VAL B 59 19.708 −11.814 −2.089 1.00 50.27 C ATOM 1404 CB VAL B 59 20.942 −10.858 −2.229 1.00 49.98 C ATOM 1405 CG1 VAL B 59 22.241 −11.607 −1.987 1.00 48.98 C ATOM 1406 CG2 VAL B 59 20.971 −10.233 −3.605 1.00 49.50 C ATOM 1407 C VAL B 59 19.732 −12.503 −0.708 1.00 51.31 C ATOM 1408 O VAL B 59 19.396 −11.889 0.306 1.00 51.41 O ATOM 1409 N ASN B 60 20.110 −13.784 −0.692 1.00 52.16 N ATOM 1410 CA ASN B 60 20.417 −14.503 0.550 1.00 52.82 C ATOM 1411 CB ASN B 60 19.494 −15.713 0.703 1.00 52.46 C ATOM 1412 CG ASN B 60 19.190 −16.052 2.165 1.00 53.85 C ATOM 1413 OD1 ASN B 60 18.162 −16.662 2.452 1.00 55.75 O ATOM 1414 ND2 ASN B 60 20.069 −15.657 3.083 1.00 51.06 N ATOM 1415 C ASN B 60 21.917 −14.916 0.621 1.00 53.15 C ATOM 1416 O ASN B 60 22.307 −16.018 0.189 1.00 53.51 O ATOM 1417 N LYS B 61 22.758 −14.024 1.159 1.00 53.07 N ATOM 1418 CA LYS B 61 24.188 −14.318 1.304 1.00 52.63 C ATOM 1419 CB LYS B 61 24.962 −13.086 1.789 1.00 52.57 C ATOM 1420 CG LYS B 61 25.168 −12.025 0.708 1.00 53.36 C ATOM 1421 CD LYS B 61 25.866 −10.798 1.240 1.00 53.65 C ATOM 1422 CE LYS B 61 26.365 −9.877 0.126 1.00 53.16 C ATOM 1423 NZ LYS B 61 27.560 −9.116 0.657 1.00 54.11 N ATOM 1424 C LYS B 61 24.443 −15.537 2.211 1.00 52.22 C ATOM 1425 O LYS B 61 25.476 −16.199 2.070 1.00 52.39 O ATOM 1426 N GLY B 62 23.489 −15.827 3.105 1.00 51.07 N ATOM 1427 CA GLY B 62 23.513 −17.025 3.955 1.00 50.34 C ATOM 1428 C GLY B 62 23.572 −18.280 3.105 1.00 49.30 C ATOM 1429 O GLY B 62 24.571 −19.021 3.116 1.00 49.51 O ATOM 1430 N SER B 63 22.498 −18.488 2.327 1.00 48.43 N ATOM 1431 CA SER B 63 22.370 −19.683 1.482 1.00 47.02 C ATOM 1432 CB SER B 63 20.884 −19.978 1.224 1.00 46.83 C ATOM 1433 OG SER B 63 20.078 −19.136 2.232 1.00 47.96 O ATOM 1434 C SER B 63 23.105 −19.552 0.135 1.00 45.91 C ATOM 1435 O SER B 63 23.128 −20.499 −0.652 1.00 45.61 O ATOM 1436 N LYS B 64 23.718 −18.402 −0.122 1.00 44.87 N ATOM 1437 CA LYS B 64 24.410 −18.152 −1.417 1.00 44.92 C ATOM 1438 CB LYS B 64 25.586 −19.115 −1.651 1.00 44.61 C ATOM 1439 CG LYS B 64 26.660 −19.099 −0.554 1.00 45.05 C ATOM 1440 CD LYS B 64 27.665 −20.213 −0.805 1.00 44.56 C ATOM 1441 CE LYS B 64 28.244 −20.755 0.486 1.00 42.89 C ATOM 1442 NZ LYS B 64 29.561 −20.185 0.780 1.00 41.38 N ATOM 1443 C LYS B 64 23.429 −18.180 −2.601 1.00 44.11 C ATOM 1444 O LYS B 64 23.754 −18.623 −3.704 1.00 44.27 O ATOM 1445 N SER B 65 22.219 −17.710 −2.358 1.00 43.78 N ATOM 1446 CA SER B 65 21.231 −17.677 −3.417 1.00 45.07 C ATOM 1447 CB SER B 65 20.157 −18.737 −3.220 1.00 45.06 C ATOM 1448 OG SER B 65 19.602 −18.635 −1.939 1.00 46.48 O ATOM 1449 C SER B 65 20.654 −16.282 −3.598 1.00 44.87 C ATOM 1450 O SER B 65 20.725 −15.444 −2.695 1.00 46.30 O ATOM 1451 N PHE B 66 20.165 −16.024 −4.795 1.00 43.98 N ATOM 1452 CA PHE B 66 19.662 −14.717 −5.174 1.00 43.45 C ATOM 1453 CB PHE B 66 20.794 −13.716 −5.484 1.00 43.22 C ATOM 1454 CG PHE B 66 21.805 −14.199 −6.486 1.00 42.41 C ATOM 1455 CD1 PHE B 66 22.667 −15.256 −6.188 1.00 41.96 C ATOM 1456 CE1 PHE B 66 23.629 −15.678 −7.083 1.00 40.78 C ATOM 1457 CZ PHE B 66 23.745 −15.037 −8.303 1.00 43.25 C ATOM 1458 CE2 PHE B 66 22.909 −13.946 −8.609 1.00 42.43 C ATOM 1459 CD2 PHE B 66 21.955 −13.537 −7.693 1.00 42.09 C ATOM 1460 C PHE B 66 18.748 −14.890 −6.362 1.00 43.59 C ATOM 1461 O PHE B 66 18.876 −15.857 −7.112 1.00 43.27 O ATOM 1462 N SER B 67 17.813 −13.966 −6.521 1.00 43.46 N ATOM 1463 CA SER B 67 16.872 −14.080 −7.599 1.00 43.95 C ATOM 1464 CB SER B 67 15.647 −14.891 −7.177 1.00 44.17 C ATOM 1465 OG SER B 67 14.969 −14.198 −6.173 1.00 47.70 O ATOM 1466 C SER B 67 16.442 −12.745 −8.140 1.00 43.18 C ATOM 1467 O SER B 67 16.571 −11.715 −7.497 1.00 42.89 O ATOM 1529 CA VAL B 75 7.276 −9.328 −26.006 1.00 45.62 C ATOM 1530 CB VAL B 75 6.624 −9.140 −27.368 1.00 45.40 C ATOM 1531 CG1 VAL B 75 5.223 −9.671 −27.324 1.00 46.53 C ATOM 1532 CG2 VAL B 75 7.440 −9.851 −28.447 1.00 45.91 C ATOM 1533 C VAL B 75 8.765 −9.030 −26.108 1.00 44.93 C ATOM 1534 O VAL B 75 9.578 −9.937 −26.234 1.00 45.36 O ATOM 1535 N GLU B 76 9.105 −7.760 −25.986 1.00 44.44 N ATOM 1536 CA GLU B 76 10.458 −7.282 −26.127 1.00 44.58 C ATOM 1537 CB GLU B 76 10.449 −5.771 −26.372 1.00 45.85 C ATOM 1538 CG GLU B 76 9.328 −5.317 −27.417 1.00 51.77 C ATOM 1539 CD GLU B 76 7.931 −5.030 −26.766 1.00 59.07 C ATOM 1540 OE1 GLU B 76 6.879 −5.154 −27.462 1.00 60.29 O ATOM 1541 OE2 GLU B 76 7.898 −4.661 −25.557 1.00 62.06 O ATOM 1542 C GLU B 76 11.389 −7.671 −24.957 1.00 43.89 C ATOM 1543 O GLU B 76 12.627 −7.513 −25.082 1.00 42.88 O ATOM 1544 N ASP B 77 10.817 −8.202 −23.859 1.00 42.42 N ATOM 1545 CA ASP B 77 11.618 −8.761 −22.766 1.00 41.98 C ATOM 1546 CB ASP B 77 10.833 −8.835 −21.468 1.00 42.23 C ATOM 1547 CG ASP B 77 10.458 −7.483 −20.905 1.00 44.50 C ATOM 1548 OD1 ASP B 77 11.179 −6.460 −21.084 1.00 48.11 O ATOM 1549 OD2 ASP B 77 9.417 −7.454 −20.227 1.00 47.95 O ATOM 1550 C ASP B 77 12.117 −10.205 −23.101 1.00 42.26 C ATOM 1551 O ASP B 77 12.839 −10.816 −22.314 1.00 42.73 O ATOM 1552 N SER B 78 11.679 −10.742 −24.230 1.00 40.74 N ATOM 1553 CA SER B 78 12.145 −12.007 −24.758 1.00 40.45 C ATOM 1554 CB SER B 78 11.467 −12.307 −26.105 1.00 37.71 C ATOM 1555 OG SER B 78 10.070 −12.574 −25.878 1.00 37.58 O ATOM 1556 C SER B 78 13.660 −11.964 −24.910 1.00 40.32 C ATOM 1557 O SER B 78 14.208 −11.100 −25.589 1.00 40.12 O ATOM 1558 N GLY B 79 14.328 −12.910 −24.280 1.00 39.35 N ATOM 1559 CA GLY B 79 15.758 −13.031 −24.490 1.00 39.80 C ATOM 1560 C GLY B 79 16.392 −13.943 −23.466 1.00 38.99 C ATOM 1561 O GLY B 79 15.697 −14.690 −22.788 1.00 39.42 O ATOM 1562 N THR B 80 17.706 −13.880 −23.381 1.00 38.30 N ATOM 1563 CA THR B 80 18.493 −14.660 −22.436 1.00 39.61 C ATOM 1564 CB THR B 80 19.765 −15.195 −23.148 1.00 39.70 C ATOM 1565 OG1 THR B 80 19.339 −16.052 −24.190 1.00 38.59 O ATOM 1566 CG2 THR B 80 20.688 −15.994 −22.197 1.00 37.90 C ATOM 1567 C THR B 80 18.929 −13.821 −21.246 1.00 40.30 C ATOM 1568 O THR B 80 19.531 −12.776 −21.414 1.00 39.92 O ATOM 1569 N TYR B 81 18.642 −14.329 −20.060 1.00 41.21 N ATOM 1570 CA TYR B 81 18.921 −13.698 −18.817 1.00 41.29 C ATOM 1571 CB TYR B 81 17.654 −13.633 −17.949 1.00 41.37 C ATOM 1572 CG TYR B 81 16.647 −12.664 −18.510 1.00 41.48 C ATOM 1573 CD1 TYR B 81 16.562 −11.381 −18.023 1.00 40.06 C ATOM 1574 CE1 TYR B 81 15.644 −10.454 −18.583 1.00 44.06 C ATOM 1575 CZ TYR B 81 14.846 −10.857 −19.675 1.00 43.01 C ATOM 1576 OH TYR B 81 13.959 −9.992 −20.249 1.00 42.85 O ATOM 1577 CE2 TYR B 81 14.913 −12.137 −20.160 1.00 37.03 C ATOM 1578 CD2 TYR B 81 15.798 −13.043 −19.604 1.00 38.04 C ATOM 1579 C TYR B 81 19.940 −14.563 −18.132 1.00 43.06 C ATOM 1580 O TYR B 81 19.798 −15.785 −18.103 1.00 43.90 O ATOM 1581 N LYS B 82 20.990 −13.924 −17.631 1.00 43.98 N ATOM 1582 CA LYS B 82 22.054 −14.585 −16.866 1.00 45.48 C ATOM 1583 CB LYS B 82 23.331 −14.667 −17.693 1.00 46.06 C ATOM 1584 CG LYS B 82 23.440 −16.011 −18.369 1.00 48.70 C ATOM 1585 CD LYS B 82 24.530 −16.006 −19.412 1.00 54.28 C ATOM 1586 CE LYS B 82 24.476 −17.315 −20.209 1.00 53.81 C ATOM 1587 NZ LYS B 82 25.735 −17.388 −20.957 1.00 57.58 N ATOM 1588 C LYS B 82 22.308 −13.867 −15.552 1.00 44.33 C ATOM 1589 O LYS B 82 22.201 −12.664 −15.484 1.00 44.79 O ATOM 1468 N LEU B 68 15.918 −12.787 −9.347 1.00 42.60 N ATOM 1469 CA LEU B 68 15.432 −11.612 −10.012 1.00 42.76 C ATOM 1470 CB LEU B 68 16.174 −11.461 −11.336 1.00 41.93 C ATOM 1471 CG LEU B 68 16.515 −10.118 −11.984 1.00 45.17 C ATOM 1472 CD1 LEU B 68 16.440 −10.205 −13.537 1.00 43.08 C ATOM 1473 CD2 LEU B 68 15.823 −8.866 −11.437 1.00 43.46 C ATOM 1474 C LEU B 68 13.988 −11.907 −10.355 1.00 42.62 C ATOM 1475 O LEU B 68 13.711 −12.896 −11.018 1.00 42.63 O ATOM 1476 N ARG B 69 13.075 −11.045 −9.973 1.00 42.71 N ATOM 1477 CA ARG B 69 11.746 −11.161 −10.528 1.00 44.20 C ATOM 1478 CB ARG B 69 10.715 −11.157 −9.418 1.00 43.82 C ATOM 1479 CG ARG B 69 9.300 −11.193 −9.930 1.00 44.98 C ATOM 1480 CD ARG B 69 8.390 −11.421 −8.752 1.00 50.13 C ATOM 1481 NE ARG B 69 7.015 −11.124 −9.113 1.00 58.36 N ATOM 1482 CZ ARG B 69 6.457 −9.914 −9.010 1.00 61.11 C ATOM 1483 NH1 ARG B 69 7.188 −8.871 −8.565 1.00 61.04 N ATOM 1484 NH2 ARG B 69 5.170 −9.750 −9.367 1.00 59.12 N ATOM 1485 C ARG B 69 11.485 −10.025 −11.500 1.00 43.87 C ATOM 1486 O ARG B 69 11.692 −8.876 −11.157 1.00 45.00 O ATOM 1487 N ILE B 70 11.026 −10.355 −12.699 1.00 43.46 N ATOM 1488 CA ILE B 70 10.727 −9.370 −13.697 1.00 43.63 C ATOM 1489 CB ILE B 70 11.407 −9.689 −15.035 1.00 45.10 C ATOM 1490 CG1 ILE B 70 12.912 −9.941 −14.806 1.00 43.18 C ATOM 1491 CD1 ILE B 70 13.478 −10.890 −15.730 1.00 45.17 C ATOM 1492 CG2 ILE B 70 11.137 −8.524 −16.012 1.00 44.11 C ATOM 1493 C ILE B 70 9.209 −9.326 −13.860 1.00 43.63 C ATOM 1494 O ILE B 70 8.592 −10.314 −14.166 1.00 43.43 O ATOM 1495 N SER B 71 8.610 −8.175 −13.579 1.00 44.13 N ATOM 1496 CA SER B 71 7.177 −8.025 −13.678 1.00 44.47 C ATOM 1497 CB SER B 71 6.659 −7.217 −12.519 1.00 43.71 C ATOM 1498 OG SER B 71 6.974 −7.938 −11.370 1.00 45.34 O ATOM 1499 C SER B 71 6.729 −7.397 −14.962 1.00 44.92 C ATOM 1500 O SER B 71 7.546 −6.909 −15.731 1.00 43.62 O ATOM 1501 N ASP B 72 5.398 −7.295 −15.068 1.00 46.93 N ATOM 1502 CA ASP B 72 4.640 −7.266 −16.317 1.00 47.72 C ATOM 1503 CB ASP B 72 3.574 −6.195 −16.338 1.00 49.50 C ATOM 1504 CG ASP B 72 4.135 −4.834 −16.302 1.00 54.38 C ATOM 1505 OD1 ASP B 72 4.521 −4.403 −15.190 1.00 60.99 O ATOM 1506 OD2 ASP B 72 4.146 −4.186 −17.381 1.00 60.20 O ATOM 1507 C ASP B 72 5.411 −7.335 −17.615 1.00 46.39 C ATOM 1508 O ASP B 72 5.706 −6.316 −18.250 1.00 46.34 O ATOM 1509 N LEU B 73 5.653 −8.569 −18.014 1.00 45.38 N ATOM 1510 CA LEU B 73 6.476 −8.921 −19.147 1.00 44.12 C ATOM 1511 CB LEU B 73 6.686 −10.447 −19.152 1.00 43.05 C ATOM 1512 CG LEU B 73 7.513 −11.022 −17.984 1.00 42.55 C ATOM 1513 CD1 LEU B 73 7.264 −12.505 −17.805 1.00 37.65 C ATOM 1514 CD2 LEU B 73 9.037 −10.729 −18.116 1.00 40.53 C ATOM 1515 C LEU B 73 5.861 −8.430 −20.443 1.00 44.58 C ATOM 1516 O LEU B 73 4.637 −8.415 −20.594 1.00 44.57 O ATOM 1517 N ARG B 74 6.712 −8.006 −21.370 1.00 44.91 N ATOM 1518 CA ARG B 74 6.279 −7.680 −22.737 1.00 45.45 C ATOM 1519 CB ARG B 74 6.565 −6.224 −23.047 1.00 45.64 C ATOM 1520 CG ARG B 74 6.164 −5.286 −22.019 1.00 49.91 C ATOM 1521 CD ARG B 74 7.106 −4.109 −22.126 1.00 57.66 C ATOM 1522 NE ARG B 74 7.462 −3.603 −20.811 1.00 60.89 N ATOM 1523 CZ ARG B 74 6.724 −2.746 −20.101 1.00 64.00 C ATOM 1524 NH1 ARG B 74 5.571 −2.278 −20.587 1.00 65.92 N ATOM 1525 NH2 ARG B 74 7.155 −2.334 −18.909 1.00 64.22 N ATOM 1526 C ARG B 74 7.067 −8.497 −23.727 1.00 44.79 C ATOM 1527 O ARG B 74 8.042 −9.136 −23.365 1.00 45.02 O ATOM 1528 N VAL B 75 6.666 −8.466 −24.983 1.00 45.42 N ATOM 1590 N CYS B 83 22.566 −14.626 −14.507 1.00 43.87 N ATOM 1591 CA CYS B 83 22.995 −14.054 −13.266 1.00 44.81 C ATOM 1592 CB CYS B 83 22.327 −14.739 −12.098 1.00 44.27 C ATOM 1593 SG CYS B 83 22.696 −16.465 −11.941 1.00 45.41 S ATOM 1594 C CYS B 83 24.497 −14.258 −13.210 1.00 46.24 C ATOM 1595 O CYS B 83 25.008 −15.105 −13.936 1.00 46.71 O ATOM 1596 N GLN B 84 25.197 −13.440 −12.415 1.00 46.76 N ATOM 1597 CA GLN B 84 26.617 −13.650 −12.077 1.00 46.51 C ATOM 1598 CB GLN B 84 27.526 −12.679 −12.810 1.00 47.55 C ATOM 1599 CG GLN B 84 29.032 −12.902 −12.495 1.00 50.71 C ATOM 1600 CD GLN B 84 29.953 −12.348 −13.563 1.00 54.90 C ATOM 1601 OE1 GLN B 84 30.999 −12.943 −13.851 1.00 61.33 O ATOM 1602 NE2 GLN B 84 29.584 −11.212 −14.160 1.00 54.98 N ATOM 1603 C GLN B 84 26.829 −13.518 −10.569 1.00 45.81 C ATOM 1604 O GLN B 84 26.324 −12.604 −9.944 1.00 44.81 O ATOM 1605 N ALA B 85 27.532 −14.488 −9.993 1.00 44.59 N ATOM 1606 CA ALA B 85 27.840 −14.484 −8.590 1.00 43.83 C ATOM 1607 CB ALA B 85 27.646 −15.884 −8.031 1.00 43.38 C ATOM 1608 C ALA B 85 29.316 −14.014 −8.479 1.00 43.84 C ATOM 1609 O ALA B 85 30.172 −14.539 −9.175 1.00 45.10 O ATOM 1610 N PHE B 86 29.603 −12.990 −7.689 1.00 43.41 N ATOM 1611 CA PHE B 86 30.985 −12.634 −7.399 1.00 43.48 C ATOM 1612 CB PHE B 86 31.195 −11.139 −7.499 1.00 43.25 C ATOM 1613 CG PHE B 86 30.922 −10.598 −8.863 1.00 45.60 C ATOM 1614 CD1 PHE B 86 29.695 −9.993 −9.153 1.00 46.99 C ATOM 1615 CE1 PHE B 86 29.434 −9.498 −10.461 1.00 49.94 C ATOM 1616 CZ PHE B 86 30.427 −9.610 −11.452 1.00 47.51 C ATOM 1617 CE2 PHE B 86 31.649 −10.207 −11.143 1.00 46.33 C ATOM 1618 CD2 PHE B 86 31.874 −10.723 −9.877 1.00 43.78 C ATOM 1619 C PHE B 86 31.291 −13.124 −6.015 1.00 44.35 C ATOM 1620 O PHE B 86 30.508 −12.925 −5.066 1.00 44.86 O ATOM 1621 N TYR B 87 32.427 −13.779 −5.866 1.00 43.59 N ATOM 1622 CA TYR B 87 32.679 −14.421 −4.604 1.00 43.44 C ATOM 1623 CB TYR B 87 32.251 −15.913 −4.633 1.00 43.50 C ATOM 1624 CG TYR B 87 32.810 −16.691 −5.817 1.00 44.45 C ATOM 1625 CD1 TYR B 87 34.022 −17.351 −5.704 1.00 46.50 C ATOM 1626 CE1 TYR B 87 34.574 −18.044 −6.759 1.00 45.78 C ATOM 1627 CZ TYR B 87 33.918 −18.111 −7.953 1.00 46.91 C ATOM 1628 OH TYR B 87 34.547 −18.831 −8.957 1.00 48.61 O ATOM 1629 CE2 TYR B 87 32.684 −17.477 −8.120 1.00 45.59 C ATOM 1630 CD2 TYR B 87 32.130 −16.777 −7.031 1.00 43.90 C ATOM 1631 C TYR B 87 34.139 −14.221 −4.248 1.00 42.55 C ATOM 1632 O TYR B 87 34.935 −13.761 −5.046 1.00 42.89 O ATOM 1633 N VAL B 88 34.468 −14.599 −3.037 1.00 41.90 N ATOM 1634 CA VAL B 88 35.747 −14.320 −2.484 1.00 40.38 C ATOM 1635 CB VAL B 88 35.563 −13.113 −1.524 1.00 41.09 C ATOM 1636 CG1 VAL B 88 36.089 −13.331 −0.157 1.00 39.39 C ATOM 1637 CG2 VAL B 88 36.117 −11.869 −2.206 1.00 41.64 C ATOM 1638 C VAL B 88 36.321 −15.611 −1.910 1.00 39.32 C ATOM 1639 O VAL B 88 35.617 −16.392 −1.274 1.00 39.48 O ATOM 1640 N PHE B 89 37.584 −15.880 −2.214 1.00 38.33 N ATOM 1641 CA PHE B 89 38.325 −16.946 −1.527 1.00 36.70 C ATOM 1642 CB PHE B 89 38.362 −18.233 −2.346 1.00 35.81 C ATOM 1643 CG PHE B 89 38.830 −18.069 −3.773 1.00 33.80 C ATOM 1644 CD1 PHE B 89 40.156 −18.343 −4.112 1.00 33.47 C ATOM 1645 CE1 PHE B 89 40.606 −18.225 −5.403 1.00 30.77 C ATOM 1646 CZ PHE B 89 39.726 −17.835 −6.426 1.00 31.68 C ATOM 1647 CE2 PHE B 89 38.387 −17.583 −6.134 1.00 33.87 C ATOM 1648 CD2 PHE B 89 37.946 −17.711 −4.782 1.00 36.04 C ATOM 1649 C PHE B 89 39.704 −16.451 −1.269 1.00 37.19 C ATOM 1650 O PHE B 89 40.059 −15.356 −1.701 1.00 36.81 O ATOM 1651 N PHE B 90 40.484 −17.258 −0.565 1.00 38.03 N ATOM 1652 CA PHE B 90 41.842 −16.928 −0.180 1.00 38.04 C ATOM 1653 CB PHE B 90 42.075 −17.297 1.280 1.00 39.75 C ATOM 1654 CG PHE B 90 41.328 −16.416 2.209 1.00 43.37 C ATOM 1655 CD1 PHE B 90 39.930 −16.435 2.223 1.00 47.99 C ATOM 1656 CE1 PHE B 90 39.208 −15.584 3.055 1.00 50.22 C ATOM 1657 CZ PHE B 90 39.893 −14.691 3.875 1.00 46.73 C ATOM 1658 CE2 PHE B 90 41.285 −14.653 3.848 1.00 49.56 C ATOM 1659 CD2 PHE B 90 41.992 −15.504 2.998 1.00 47.02 C ATOM 1660 C PHE B 90 42.831 −17.568 −1.103 1.00 37.73 C ATOM 1661 O PHE B 90 42.675 −18.723 −1.455 1.00 35.86 O ATOM 1662 N ALA B 91 43.808 −16.766 −1.541 1.00 38.81 N ATOM 1663 CA ALA B 91 44.880 −17.186 −2.450 1.00 41.01 C ATOM 1664 CB ALA B 91 45.887 −16.050 −2.613 1.00 41.04 C ATOM 1665 C ALA B 91 45.610 −18.459 −1.997 1.00 42.55 C ATOM 1666 O ALA B 91 46.126 −19.208 −2.826 1.00 41.40 O ATOM 1667 N GLU B 92 45.643 −18.675 −0.677 1.00 45.64 N ATOM 1668 CA GLU B 92 46.278 −19.854 −0.067 1.00 49.34 C ATOM 1669 CB GLU B 92 46.339 −19.765 1.468 1.00 49.34 C ATOM 1670 CG GLU B 92 47.103 −18.578 2.047 1.00 53.21 C ATOM 1671 CD GLU B 92 46.215 −17.331 2.266 1.00 57.21 C ATOM 1672 OE1 GLU B 92 45.848 −17.086 3.448 1.00 59.01 O ATOM 1673 OE2 GLU B 92 45.901 −16.599 1.280 1.00 55.91 O ATOM 1674 C GLU B 92 45.529 −21.121 −0.433 1.00 50.92 C ATOM 1675 O GLU B 92 46.163 −22.112 −0.803 1.00 51.36 O ATOM 1676 N ASP B 93 44.198 −21.098 −0.315 1.00 52.93 N ATOM 1677 CA ASP B 93 43.454 −22.356 −0.337 1.00 55.69 C ATOM 1678 CB ASP B 93 41.992 −22.280 0.238 1.00 55.85 C ATOM 1679 CG ASP B 93 40.982 −21.501 −0.651 1.00 58.02 C ATOM 1680 OD1 ASP B 93 40.972 −21.667 −1.896 1.00 60.03 O ATOM 1681 OD2 ASP B 93 40.134 −20.749 −0.080 1.00 58.21 O ATOM 1682 C ASP B 93 43.647 −23.117 −1.659 1.00 57.09 C ATOM 1683 O ASP B 93 43.222 −22.670 −2.731 1.00 56.60 O ATOM 1684 N VAL B 94 44.381 −24.231 −1.542 1.00 59.08 N ATOM 1685 CA VAL B 94 44.863 −25.029 −2.673 1.00 61.07 C ATOM 1686 CB VAL B 94 46.088 −25.913 −2.271 1.00 61.32 C ATOM 1687 CG1 VAL B 94 46.489 −26.881 −3.404 1.00 61.77 C ATOM 1688 CG2 VAL B 94 47.300 −25.062 −1.795 1.00 61.40 C ATOM 1689 C VAL B 94 43.755 −25.952 −3.125 1.00 62.29 C ATOM 1690 O VAL B 94 42.925 −26.361 −2.312 1.00 62.77 O ATOM 1691 N GLY B 95 43.738 −26.286 −4.410 1.00 63.72 N ATOM 1692 CA GLY B 95 42.849 −27.341 −4.889 1.00 65.63 C ATOM 1693 C GLY B 95 41.366 −26.996 −4.820 1.00 66.94 C ATOM 1694 O GLY B 95 40.503 −27.897 −4.790 1.00 67.35 O ATOM 1695 N SER B 96 41.082 −25.693 −4.764 1.00 67.66 N ATOM 1696 CA SER B 96 39.752 −25.126 −5.019 1.00 68.33 C ATOM 1697 CB SER B 96 38.719 −25.490 −3.934 1.00 68.30 C ATOM 1698 OG SER B 96 39.096 −25.003 −2.655 1.00 69.15 O ATOM 1699 C SER B 96 39.951 −23.610 −5.149 1.00 68.57 C ATOM 1700 O SER B 96 40.232 −22.909 −4.161 1.00 68.47 O ATOM 1701 N ASN B 97 39.872 −23.144 −6.399 1.00 68.54 N ATOM 1702 CA ASN B 97 40.063 −21.737 −6.798 1.00 67.90 C ATOM 1703 CB ASN B 97 41.539 −21.450 −7.190 1.00 67.64 C ATOM 1704 CG ASN B 97 42.549 −21.839 −6.102 1.00 67.80 C ATOM 1705 OD1 ASN B 97 43.346 −21.010 −5.642 1.00 68.17 O ATOM 1706 ND2 ASN B 97 42.535 −23.103 −5.706 1.00 67.46 N ATOM 1707 C ASN B 97 39.164 −21.548 −8.020 1.00 67.37 C ATOM 1708 O ASN B 97 39.474 −20.763 −8.918 1.00 67.83 O ATOM 1709 N LYS B 98 38.028 −22.246 −8.012 1.00 66.43 N ATOM 1710 CA LYS B 98 37.501 −22.902 −9.221 1.00 65.41 C ATOM 1711 CB LYS B 98 36.489 −24.003 −8.837 1.00 65.75 C ATOM 1712 CG LYS B 98 37.167 −25.283 −8.285 1.00 67.70 C ATOM 1713 CD LYS B 98 36.292 −26.019 −7.266 1.00 70.57 C ATOM 1714 CE LYS B 98 36.108 −25.188 −5.992 1.00 71.50 C ATOM 1715 NZ LYS B 98 35.816 −26.004 −4.778 1.00 71.51 N ATOM 1716 C LYS B 98 37.036 −22.104 −10.467 1.00 64.00 C ATOM 1717 O LYS B 98 37.100 −22.642 −11.587 1.00 64.50 O ATOM 1718 N GLY B 99 36.583 −20.861 −10.313 1.00 61.92 N ATOM 1719 CA GLY B 99 35.934 −20.173 −11.453 1.00 58.65 C ATOM 1720 C GLY B 99 36.850 −19.277 −12.268 1.00 56.59 C ATOM 1721 O GLY B 99 38.048 −19.538 −12.374 1.00 56.84 O ATOM 1722 N ALA B 100 36.282 −18.223 −12.849 1.00 53.87 N ATOM 1723 CA ALA B 100 37.065 −17.133 −13.429 1.00 51.62 C ATOM 1724 CB ALA B 100 36.164 −16.245 −14.269 1.00 51.17 C ATOM 1725 C ALA B 100 37.690 −16.294 −12.312 1.00 49.55 C ATOM 1726 O ALA B 100 36.987 −15.896 −11.373 1.00 49.34 O ATOM 1727 N ILE B 101 38.985 −16.005 −12.395 1.00 47.31 N ATOM 1728 CA ILE B 101 39.533 −14.981 −11.484 1.00 45.25 C ATOM 1729 CB ILE B 101 40.904 −15.345 −10.756 1.00 45.80 C ATOM 1730 CG1 ILE B 101 42.016 −14.358 −11.079 1.00 46.05 C ATOM 1731 CD1 ILE B 101 42.324 −13.495 −9.928 1.00 46.13 C ATOM 1732 CG2 ILE B 101 41.319 −16.849 −10.843 1.00 44.18 C ATOM 1733 C ILE B 101 39.355 −13.542 −12.031 1.00 44.02 C ATOM 1734 O ILE B 101 39.651 −13.227 −13.209 1.00 43.07 O ATOM 1735 N ILE B 102 38.734 −12.724 −11.185 1.00 41.55 N ATOM 1736 CA ILE B 102 38.307 −11.368 −11.482 1.00 40.42 C ATOM 1737 CB ILE B 102 36.935 −11.028 −10.777 1.00 41.20 C ATOM 1738 CG1 ILE B 102 35.748 −11.863 −11.308 1.00 43.88 C ATOM 1739 CD1 ILE B 102 35.773 −12.274 −12.825 1.00 43.26 C ATOM 1740 CG2 ILE B 102 36.582 −9.531 −10.871 1.00 44.23 C ATOM 1741 C ILE B 102 39.378 −10.376 −10.971 1.00 39.32 C ATOM 1742 O ILE B 102 39.623 −9.342 −11.614 1.00 39.71 O ATOM 1743 N GLY B 103 40.002 −10.670 −9.810 1.00 36.32 N ATOM 1744 CA GLY B 103 41.079 −9.842 −9.312 1.00 32.38 C ATOM 1745 C GLY B 103 41.673 −10.369 −8.038 1.00 31.16 C ATOM 1746 O GLY B 103 41.199 −11.372 −7.457 1.00 31.39 O ATOM 1747 N LEU B 104 42.706 −9.670 −7.578 1.00 29.03 N ATOM 1748 CA LEU B 104 43.424 −10.049 −6.423 1.00 27.58 C ATOM 1749 CB LEU B 104 44.839 −10.544 −6.818 1.00 26.53 C ATOM 1750 CG LEU B 104 45.829 −10.943 −5.733 1.00 26.78 C ATOM 1751 CD1 LEU B 104 47.232 −11.015 −6.252 1.00 30.47 C ATOM 1752 CD2 LEU B 104 45.473 −12.251 −5.078 1.00 27.53 C ATOM 1753 C LEU B 104 43.459 −8.841 −5.496 1.00 28.83 C ATOM 1754 O LEU B 104 43.870 −7.752 −5.901 1.00 27.59 O ATOM 1755 N MET B 105 43.067 −9.055 −4.233 1.00 29.96 N ATOM 1756 CA MET B 105 43.136 −8.031 −3.177 1.00 31.39 C ATOM 1757 CB MET B 105 41.918 −8.182 −2.270 1.00 33.00 C ATOM 1758 CG MET B 105 41.063 −6.942 −2.145 1.00 38.80 C ATOM 1759 SD MET B 105 40.356 −6.594 −3.753 1.00 41.80 S ATOM 1760 CE MET B 105 39.143 −7.874 −3.693 1.00 49.56 C ATOM 1761 C MET B 105 44.336 −8.189 −2.319 1.00 31.71 C ATOM 1762 O MET B 105 44.667 −9.305 −1.911 1.00 31.15 O ATOM 1763 N VAL B 106 44.991 −7.075 −2.006 1.00 31.47 N ATOM 1764 CA VAL B 106 45.960 −7.056 −0.929 1.00 33.12 C ATOM 1765 CB VAL B 106 46.528 −5.649 −0.736 1.00 32.05 C ATOM 1766 CG1 VAL B 106 47.526 −5.649 0.323 1.00 32.12 C ATOM 1767 CG2 VAL B 106 47.164 −5.186 −2.013 1.00 31.80 C ATOM 1768 C VAL B 106 45.287 −7.601 0.368 1.00 34.62 C ATOM 1769 O VAL B 106 44.032 −7.384 0.577 1.00 34.28 O ATOM 1770 N GLY B 107 46.126 −8.309 1.212 1.00 34.95 N ATOM 1771 CA GLY B 107 45.566 −9.209 2.267 1.00 34.64 C ATOM 1772 C GLY B 107 45.048 −10.613 1.825 1.00 35.04 C ATOM 1773 O GLY B 107 44.566 −11.404 2.676 1.00 36.55 O ATOM 1774 N GLY B 108 45.122 −10.929 0.525 1.00 32.55 N ATOM 1775 CA GLY B 108 45.225 −12.307 0.075 1.00 30.81 C ATOM 1776 C GLY B 108 43.925 −12.886 −0.359 1.00 30.73 C ATOM 1777 O GLY B 108 43.812 −14.091 −0.489 1.00 31.42 O ATOM 1778 N VAL B 109 42.963 −12.006 −0.622 1.00 30.06 N ATOM 1779 CA VAL B 109 41.610 −12.332 −1.113 1.00 29.98 C ATOM 1780 CB VAL B 109 40.595 −11.330 −0.447 1.00 29.82 C ATOM 1781 CG1 VAL B 109 39.238 −11.415 −0.954 1.00 27.30 C ATOM 1782 CG2 VAL B 109 40.579 −11.519 1.073 1.00 31.58 C ATOM 1783 C VAL B 109 41.576 −12.271 −2.652 1.00 30.22 C ATOM 1784 O VAL B 109 41.988 −11.285 −3.280 1.00 29.55 O ATOM 1785 N VAL B 110 41.103 −13.354 −3.257 1.00 31.00 N ATOM 1786 CA VAL B 110 40.832 −13.376 −4.656 1.00 30.34 C ATOM 1787 CB VAL B 110 41.760 −14.318 −5.501 1.00 30.78 C ATOM 1788 CG1 VAL B 110 41.079 −14.939 −6.663 1.00 27.57 C ATOM 1789 CG2 VAL B 110 42.605 −15.240 −4.676 1.00 28.92 C ATOM 1790 C VAL B 110 39.376 −13.342 −4.934 1.00 32.42 C ATOM 1791 O VAL B 110 38.617 −13.904 −4.193 1.00 32.63 O ATOM 1792 N ILE B 111 38.986 −12.596 −5.962 1.00 34.25 N ATOM 1793 CA ILE B 111 37.608 −12.418 −6.360 1.00 36.25 C ATOM 1794 CB ILE B 111 37.377 −10.966 −6.834 1.00 37.63 C ATOM 1795 CG1 ILE B 111 38.177 −9.980 −5.960 1.00 39.86 C ATOM 1796 CD1 ILE B 111 37.582 −9.749 −4.568 1.00 44.15 C ATOM 1797 CG2 ILE B 111 35.871 −10.598 −6.970 1.00 35.86 C ATOM 1798 C ILE B 111 37.401 −13.299 −7.581 1.00 37.45 C ATOM 1799 O ILE B 111 38.116 −13.150 −8.569 1.00 38.10 O ATOM 1800 N GLY B 112 36.478 −14.244 −7.487 1.00 37.85 N ATOM 1801 CA GLY B 112 36.044 −15.026 −8.625 1.00 39.55 C ATOM 1802 C GLY B 112 34.660 −14.536 −9.031 1.00 40.92 C ATOM 1803 O GLY B 112 33.991 −13.833 −8.279 1.00 40.69 O ATOM 1804 N GLY B 113 34.240 −14.877 −10.241 1.00 41.72 N ATOM 1805 CA GLY B 113 32.878 −14.675 −10.631 1.00 42.68 C ATOM 1806 C GLY B 113 32.526 −15.932 −11.369 1.00 44.53 C ATOM 1807 O GLY B 113 33.385 −16.523 −12.033 1.00 45.28 O ATOM 1808 N GLU B 114 31.281 −16.352 −11.230 1.00 45.00 N ATOM 1809 CA GLU B 114 30.721 −17.475 −11.954 1.00 46.79 C ATOM 1810 CB GLU B 114 30.486 −18.650 −11.003 1.00 47.57 C ATOM 1811 CG GLU B 114 31.481 −19.777 −11.016 1.00 54.05 C ATOM 1812 CD GLU B 114 31.681 −20.428 −12.384 1.00 60.74 C ATOM 1813 OE1 GLU B 114 32.730 −21.116 −12.540 1.00 65.24 O ATOM 1814 OE2 GLU B 114 30.834 −20.241 −13.294 1.00 62.06 O ATOM 1815 C GLU B 114 29.349 −16.990 −12.451 1.00 46.24 C ATOM 1816 O GLU B 114 28.600 −16.427 −11.683 1.00 45.45 O ATOM 1817 N LYS B 115 29.048 −17.210 −13.730 1.00 47.57 N ATOM 1818 CA LYS B 115 27.705 −16.986 −14.306 1.00 47.63 C ATOM 1819 CB LYS B 115 27.868 −16.442 −15.716 1.00 49.05 C ATOM 1820 CG LYS B 115 28.285 −14.990 −15.769 1.00 49.49 C ATOM 1821 CD LYS B 115 28.457 −14.608 −17.209 1.00 58.06 C ATOM 1822 CE LYS B 115 28.325 −13.100 −17.425 1.00 62.98 C ATOM 1823 NZ LYS B 115 29.569 −12.371 −16.971 1.00 67.39 N ATOM 1824 C LYS B 115 26.831 −18.235 −14.341 1.00 46.96 C ATOM 1825 O LYS B 115 27.328 −19.359 −14.475 1.00 46.33 O ATOM 1826 N GLY B 116 25.522 −18.055 −14.202 1.00 46.82 N ATOM 1827 CA GLY B 116 24.551 −19.156 −14.429 1.00 45.94 C ATOM 1828 C GLY B 116 24.477 −19.549 −15.896 1.00 46.06 C ATOM 1829 O GLY B 116 24.948 −18.798 −16.764 1.00 46.74 O ATOM 1830 N ALA B 117 23.929 −20.732 −16.203 1.00 44.78 N ATOM 1831 CA ALA B 117 23.856 −21.181 −17.602 1.00 43.54 C ATOM 1832 CB ALA B 117 23.609 −22.733 −17.710 1.00 42.15 C ATOM 1833 C ALA B 117 22.804 −20.377 −18.395 1.00 43.36 C ATOM 1834 O ALA B 117 22.765 −20.473 −19.619 1.00 44.57 O ATOM 1835 N GLY B 118 22.009 −19.543 −17.711 1.00 42.01 N ATOM 1836 CA GLY B 118 21.041 −18.672 −18.374 1.00 40.50 C ATOM 1837 C GLY B 118 19.638 −19.226 −18.447 1.00 40.45 C ATOM 1838 O GLY B 118 19.440 −20.454 −18.385 1.00 39.63 O ATOM 1839 N THR B 119 18.689 −18.293 −18.609 1.00 39.73 N ATOM 1840 CA THR B 119 17.267 −18.517 −18.728 1.00 39.06 C ATOM 1841 CB THR B 119 16.494 −17.767 −17.648 1.00 39.37 C ATOM 1842 OG1 THR B 119 16.867 −18.298 −16.359 1.00 42.58 O ATOM 1843 CG2 THR B 119 14.985 −17.926 −17.817 1.00 36.37 C ATOM 1844 C THR B 119 16.846 −18.000 −20.086 1.00 40.30 C ATOM 1845 O THR B 119 17.046 −16.827 −20.386 1.00 40.23 O ATOM 1846 N ALA B 120 16.306 −18.881 −20.930 1.00 40.46 N ATOM 1847 CA ALA B 120 15.808 −18.450 −22.232 1.00 39.96 C ATOM 1848 CB ALA B 120 16.032 −19.546 −23.327 1.00 38.10 C ATOM 1849 C ALA B 120 14.333 −18.107 −22.056 1.00 39.39 C ATOM 1850 O ALA B 120 13.514 −18.995 −21.874 1.00 39.29 O ATOM 1851 N LEU B 121 14.018 −16.811 −22.058 1.00 38.26 N ATOM 1852 CA LEU B 121 12.655 −16.366 −21.893 1.00 38.37 C ATOM 1853 CB LEU B 121 12.552 −15.321 −20.816 1.00 37.24 C ATOM 1854 CG LEU B 121 11.223 −14.563 −20.800 1.00 39.25 C ATOM 1855 CD1 LEU B 121 10.056 −15.389 −20.199 1.00 38.60 C ATOM 1856 CD2 LEU B 121 11.327 −13.202 −20.149 1.00 34.33 C ATOM 1857 C LEU B 121 11.955 −15.883 −23.237 1.00 39.04 C ATOM 1858 O LEU B 121 12.473 −15.020 −23.955 1.00 40.91 O ATOM 1859 N THR B 122 10.811 −16.491 −23.548 1.00 38.34 N ATOM 1860 CA THR B 122 9.930 −16.055 −24.614 1.00 39.43 C ATOM 1861 CB THR B 122 9.552 −17.214 −25.559 1.00 39.02 C ATOM 1862 OG1 THR B 122 10.738 −17.917 −25.949 1.00 39.58 O ATOM 1863 CG2 THR B 122 8.846 −16.654 −26.785 1.00 40.51 C ATOM 1864 C THR B 122 8.660 −15.512 −23.988 1.00 38.05 C ATOM 1865 O THR B 122 8.034 −16.192 −23.186 1.00 38.30 O ATOM 1866 N VAL B 123 8.343 −14.258 −24.283 1.00 38.09 N ATOM 1867 CA VAL B 123 7.093 −13.650 −23.812 1.00 38.38 C ATOM 1868 CB VAL B 123 7.274 −12.260 −23.225 1.00 37.30 C ATOM 1869 CG1 VAL B 123 5.940 −11.665 −22.754 1.00 38.24 C ATOM 1870 CG2 VAL B 123 8.307 −12.240 −22.120 1.00 35.68 C ATOM 1871 C VAL B 123 6.172 −13.609 −25.055 1.00 40.09 C ATOM 1872 O VAL B 123 6.580 −13.168 −26.152 1.00 38.15 O ATOM 1873 N LYS B 124 4.948 −14.096 −24.870 1.00 42.46 N ATOM 1874 CA LYS B 124 3.962 −14.184 −25.947 1.00 45.11 C ATOM 1875 CB LYS B 124 3.596 −15.645 −26.162 1.00 44.65 C ATOM 1876 CG LYS B 124 4.855 −16.487 −26.597 1.00 44.00 C ATOM 1877 CD LYS B 124 4.562 −17.860 −27.095 1.00 41.77 C ATOM 1878 CE LYS B 124 5.855 −18.519 −27.544 1.00 40.51 C ATOM 1879 NZ LYS B 124 5.576 −19.819 −28.207 1.00 47.63 N ATOM 1880 C LYS B 124 2.734 −13.382 −25.557 1.00 47.91 C ATOM 1881 O LYS B 124 2.298 −13.441 −24.407 1.00 48.54 O ATOM 1882 N ALA B 125 2.192 −12.603 −26.488 1.00 50.80 N ATOM 1883 CA ALA B 125 0.849 −12.034 −26.276 1.00 53.80 C ATOM 1884 CB ALA B 125 0.556 −10.903 −27.275 1.00 53.63 C ATOM 1885 C ALA B 125 −0.163 −13.137 −26.440 1.00 55.22 C ATOM 1886 O ALA B 125 −0.164 −13.791 −27.472 1.00 56.23 O ATOM 1887 N ALA B 126 −1.002 −13.379 −25.438 1.00 57.49 N ATOM 1888 CA ALA B 126 −2.254 −14.133 −25.698 1.00 59.24 C ATOM 1889 CB ALA B 126 −3.063 −14.300 −24.393 1.00 59.45 C ATOM 1890 C ALA B 126 −3.111 −13.414 −26.810 1.00 60.27 C ATOM 1891 O ALA B 126 −3.505 −13.983 −27.865 1.00 59.50 O ATOM 1892 OXT ALA B 126 −3.391 −12.183 −26.675 1.00 60.56 O ATOM 1893 N ALA C 1 47.894 12.704 −2.969 1.00 49.41 N ATOM 1894 CA ALA C 1 46.483 12.845 −2.525 1.00 48.69 C ATOM 1895 CB ALA C 1 45.612 11.926 −3.320 1.00 49.22 C ATOM 1896 C ALA C 1 46.345 12.555 −1.040 1.00 49.03 C ATOM 1897 O ALA C 1 47.219 11.950 −0.422 1.00 48.45 O ATOM 1898 N TRP C 2 45.241 12.989 −0.442 1.00 48.83 N ATOM 1899 CA TRP C 2 45.029 12.703 0.970 1.00 47.92 C ATOM 1900 CB TRP C 2 45.920 13.592 1.858 1.00 46.22 C ATOM 1901 CG TRP C 2 45.728 15.092 1.734 1.00 46.85 C ATOM 1902 CD1 TRP C 2 46.068 15.895 0.653 1.00 46.02 C ATOM 1903 NE1 TRP C 2 45.753 17.216 0.924 1.00 45.63 N ATOM 1904 CE2 TRP C 2 45.233 17.303 2.191 1.00 46.81 C ATOM 1905 CD2 TRP C 2 45.200 15.983 2.737 1.00 47.63 C ATOM 1906 CE3 TRP C 2 44.719 15.802 4.053 1.00 46.87 C ATOM 1907 CZ3 TRP C 2 44.289 16.918 4.769 1.00 46.19 C ATOM 1908 CH2 TRP C 2 44.326 18.226 4.185 1.00 45.94 C ATOM 1909 CZ2 TRP C 2 44.781 18.428 2.907 1.00 46.39 C ATOM 1910 C TRP C 2 43.560 12.862 1.314 1.00 48.15 C ATOM 1911 O TRP C 2 42.877 13.673 0.702 1.00 47.92 O ATOM 1912 N VAL C 3 43.077 12.104 2.304 1.00 48.14 N ATOM 1913 CA VAL C 3 41.713 12.343 2.793 1.00 47.09 C ATOM 1914 CB VAL C 3 40.905 11.060 3.039 1.00 46.72 C ATOM 1915 CG1 VAL C 3 39.538 11.402 3.680 1.00 44.65 C ATOM 1916 CG2 VAL C 3 40.706 10.367 1.753 1.00 46.02 C ATOM 1917 C VAL C 3 41.738 13.261 3.993 1.00 46.31 C ATOM 1918 O VAL C 3 42.494 13.073 4.925 1.00 48.10 O ATOM 1919 N ASP C 4 40.937 14.303 3.930 1.00 46.31 N ATOM 1920 CA ASP C 4 40.908 15.306 4.965 1.00 45.27 C ATOM 1921 CB ASP C 4 40.916 16.681 4.312 1.00 45.16 C ATOM 1922 CG ASP C 4 40.888 17.815 5.312 1.00 46.64 C ATOM 1923 OD1 ASP C 4 41.135 17.640 6.526 1.00 52.47 O ATOM 1924 OD2 ASP C 4 40.594 18.933 4.886 1.00 48.46 O ATOM 1925 C ASP C 4 39.615 15.025 5.728 1.00 44.41 C ATOM 1926 O ASP C 4 38.534 15.276 5.260 1.00 43.86 O ATOM 1927 N GLN C 5 39.777 14.424 6.883 1.00 43.38 N ATOM 1928 CA GLN C 5 38.699 14.020 7.725 1.00 42.49 C ATOM 1929 CB GLN C 5 38.951 12.585 8.184 1.00 43.25 C ATOM 1930 CG GLN C 5 37.964 12.087 9.266 1.00 42.78 C ATOM 1931 CD GLN C 5 38.117 10.629 9.568 1.00 43.36 C ATOM 1932 OE1 GLN C 5 38.975 9.911 8.977 1.00 44.25 O ATOM 1933 NE2 GLN C 5 37.341 10.171 10.522 1.00 41.48 N ATOM 1934 C GLN C 5 38.612 14.947 8.919 1.00 41.74 C ATOM 1935 O GLN C 5 39.573 15.107 9.659 1.00 41.18 O ATOM 1936 N THR C 6 37.434 15.557 9.077 1.00 42.37 N ATOM 1937 CA THR C 6 37.127 16.448 10.187 1.00 42.38 C ATOM 1938 CB THR C 6 37.134 17.922 9.730 1.00 43.81 C ATOM 1939 OG1 THR C 6 36.323 18.087 8.567 1.00 42.52 O ATOM 1940 CG2 THR C 6 38.614 18.342 9.375 1.00 41.50 C ATOM 1941 C THR C 6 35.801 16.006 10.801 1.00 42.03 C ATOM 1942 O THR C 6 34.967 15.469 10.102 1.00 42.87 O ATOM 1943 N PRO C 7 35.654 16.121 12.134 1.00 41.26 N ATOM 1944 CA PRO C 7 36.674 16.605 13.095 1.00 39.68 C ATOM 1945 CB PRO C 7 35.847 17.012 14.318 1.00 38.19 C ATOM 1946 CG PRO C 7 34.571 16.163 14.235 1.00 39.85 C ATOM 1947 CD PRO C 7 34.370 15.774 12.795 1.00 41.08 C ATOM 1948 C PRO C 7 37.674 15.539 13.526 1.00 40.17 C ATOM 1949 O PRO C 7 37.376 14.341 13.492 1.00 40.26 O ATOM 1950 N ARG C 8 38.833 15.968 14.000 1.00 39.86 N ATOM 1951 CA ARG C 8 39.787 15.015 14.450 1.00 42.27 C ATOM 1952 CB ARG C 8 41.170 15.678 14.495 1.00 43.98 C ATOM 1953 CG ARG C 8 42.321 14.715 14.708 1.00 50.28 C ATOM 1954 CD ARG C 8 42.501 13.799 13.469 1.00 56.99 C ATOM 1955 NE ARG C 8 43.131 14.492 12.357 1.00 59.34 N ATOM 1956 CZ ARG C 8 44.447 14.636 12.274 1.00 64.10 C ATOM 1957 NH1 ARG C 8 45.012 15.284 11.252 1.00 65.07 N ATOM 1958 NH2 ARG C 8 45.200 14.117 13.239 1.00 67.46 N ATOM 1959 C ARG C 8 39.357 14.418 15.816 1.00 41.81 C ATOM 1960 O ARG C 8 39.638 13.250 16.123 1.00 41.61 O ATOM 1961 N THR C 9 38.647 15.208 16.622 1.00 41.23 N ATOM 1962 CA THR C 9 38.189 14.769 17.918 1.00 41.41 C ATOM 1963 CB THR C 9 39.112 15.257 19.097 1.00 42.45 C ATOM 1964 OG1 THR C 9 39.108 16.701 19.180 1.00 45.56 O ATOM 1965 CG2 THR C 9 40.515 14.757 18.961 1.00 40.73 C ATOM 1966 C THR C 9 36.847 15.389 18.127 1.00 41.08 C ATOM 1967 O THR C 9 36.648 16.543 17.778 1.00 42.09 O ATOM 1968 N ALA C 10 35.932 14.635 18.707 1.00 40.39 N ATOM 1969 CA ALA C 10 34.587 15.110 19.081 1.00 40.33 C ATOM 1970 CB ALA C 10 33.522 14.620 18.072 1.00 38.32 C ATOM 1971 C ALA C 10 34.259 14.568 20.473 1.00 41.20 C ATOM 1972 O ALA C 10 34.525 13.384 20.784 1.00 40.94 O ATOM 1973 N THR C 11 33.736 15.455 21.324 1.00 42.57 N ATOM 1974 CA THR C 11 33.123 15.099 22.616 1.00 42.23 C ATOM 1975 CB THR C 11 33.759 15.861 23.749 1.00 42.79 C ATOM 1976 OG1 THR C 11 35.145 15.491 23.827 1.00 46.26 O ATOM 1977 CG2 THR C 11 33.078 15.537 25.097 1.00 40.59 C ATOM 1978 C THR C 11 31.633 15.460 22.493 1.00 42.65 C ATOM 1979 O THR C 11 31.325 16.618 22.223 1.00 43.18 O ATOM 1980 N LYS C 12 30.743 14.467 22.657 1.00 41.78 N ATOM 1981 CA LYS C 12 29.339 14.597 22.369 1.00 41.37 C ATOM 1982 CB LYS C 12 28.928 13.733 21.191 1.00 41.59 C ATOM 1983 CG LYS C 12 29.465 14.167 19.826 1.00 41.91 C ATOM 1984 CD LYS C 12 29.346 15.654 19.576 1.00 43.02 C ATOM 1985 CE LYS C 12 28.977 15.936 18.151 1.00 46.80 C ATOM 1986 NZ LYS C 12 29.307 17.320 17.716 1.00 49.30 N ATOM 1987 C LYS C 12 28.579 14.096 23.536 1.00 42.56 C ATOM 1988 O LYS C 12 29.097 13.230 24.256 1.00 43.65 O ATOM 1989 N GLU C 13 27.341 14.602 23.726 1.00 41.23 N ATOM 1990 CA GLU C 13 26.474 14.080 24.762 1.00 41.54 C ATOM 1991 CB GLU C 13 25.675 15.232 25.379 1.00 41.00 C ATOM 1992 CG GLU C 13 26.562 16.359 25.900 1.00 42.17 C ATOM 1993 CD GLU C 13 25.723 17.635 26.233 1.00 46.00 C ATOM 1994 OE1 GLU C 13 26.311 18.695 26.591 1.00 47.15 O ATOM 1995 OE2 GLU C 13 24.466 17.550 26.116 1.00 48.60 O ATOM 1996 C GLU C 13 25.563 13.073 24.149 1.00 40.75 C ATOM 1997 O GLU C 13 25.335 13.105 22.910 1.00 42.27 O ATOM 1998 N THR C 14 25.002 12.167 24.938 1.00 40.94 N ATOM 1999 CA THR C 14 24.042 11.239 24.328 1.00 42.25 C ATOM 2000 CB THR C 14 23.544 10.101 25.272 1.00 42.73 C ATOM 2001 OG1 THR C 14 22.715 10.665 26.243 1.00 48.01 O ATOM 2002 CG2 THR C 14 24.705 9.386 25.975 1.00 42.04 C ATOM 2003 C THR C 14 22.861 12.015 23.700 1.00 40.89 C ATOM 2004 O THR C 14 22.487 13.053 24.202 1.00 41.70 O ATOM 2005 N GLY C 15 22.308 11.538 22.591 1.00 39.88 N ATOM 2006 CA GLY C 15 21.224 12.239 21.898 1.00 38.62 C ATOM 2007 C GLY C 15 21.690 13.211 20.812 1.00 38.27 C ATOM 2008 O GLY C 15 20.912 13.537 19.886 1.00 39.29 O ATOM 2009 N GLU C 16 22.921 13.685 20.902 1.00 36.77 N ATOM 2010 CA GLU C 16 23.522 14.515 19.858 1.00 38.21 C ATOM 2011 CB GLU C 16 24.766 15.286 20.373 1.00 37.37 C ATOM 2012 CG GLU C 16 24.448 16.420 21.495 1.00 38.40 C ATOM 2013 CD GLU C 16 25.627 17.359 21.780 1.00 38.50 C ATOM 2014 OE1 GLU C 16 26.733 16.846 21.984 1.00 40.44 O ATOM 2015 OE2 GLU C 16 25.489 18.609 21.757 1.00 38.88 O ATOM 2016 C GLU C 16 23.874 13.652 18.635 1.00 40.24 C ATOM 2017 O GLU C 16 23.852 12.414 18.745 1.00 42.05 O ATOM 2018 N SER C 17 24.137 14.306 17.494 1.00 39.57 N ATOM 2019 CA SER C 17 24.621 13.722 16.264 1.00 40.14 C ATOM 2020 CB SER C 17 23.844 14.317 15.073 1.00 39.97 C ATOM 2021 OG SER C 17 22.451 13.972 15.174 1.00 42.60 O ATOM 2022 C SER C 17 26.094 14.113 16.057 1.00 40.75 C ATOM 2023 O SER C 17 26.547 15.102 16.557 1.00 40.20 O ATOM 2024 N LEU C 18 26.823 13.314 15.288 1.00 40.85 N ATOM 2025 CA LEU C 18 28.139 13.643 14.874 1.00 41.38 C ATOM 2026 CB LEU C 18 29.061 12.561 15.427 1.00 41.14 C ATOM 2027 CG LEU C 18 30.600 12.596 15.451 1.00 44.10 C ATOM 2028 CD1 LEU C 18 31.251 11.259 14.907 1.00 38.99 C ATOM 2029 CD2 LEU C 18 31.291 13.933 15.015 1.00 41.87 C ATOM 2030 C LEU C 18 28.102 13.544 13.321 1.00 41.20 C ATOM 2031 O LEU C 18 27.616 12.564 12.803 1.00 39.57 O ATOM 2032 N THR C 19 28.624 14.567 12.624 1.00 41.23 N ATOM 2033 CA THR C 19 28.945 14.495 11.209 1.00 41.67 C ATOM 2034 CB THR C 19 28.303 15.664 10.371 1.00 41.81 C ATOM 2035 OG1 THR C 19 26.939 15.741 10.732 1.00 41.36 O ATOM 2036 CG2 THR C 19 28.390 15.426 8.826 1.00 41.66 C ATOM 2037 C THR C 19 30.442 14.493 11.061 1.00 41.89 C ATOM 2038 O THR C 19 31.144 15.426 11.504 1.00 41.70 O ATOM 2039 N ILE C 20 30.930 13.399 10.473 1.00 41.66 N ATOM 2040 CA ILE C 20 32.321 13.291 10.062 1.00 42.12 C ATOM 2041 CB ILE C 20 32.855 11.887 10.306 1.00 41.88 C ATOM 2042 CG1 ILE C 20 32.758 11.550 11.820 1.00 41.13 C ATOM 2043 CD1 ILE C 20 32.960 10.088 12.166 1.00 40.95 C ATOM 2044 CG2 ILE C 20 34.363 11.820 9.859 1.00 42.36 C ATOM 2045 C ILE C 20 32.348 13.605 8.568 1.00 42.26 C ATOM 2046 O ILE C 20 31.661 12.949 7.823 1.00 41.71 O ATOM 2047 N ASN C 21 33.104 14.624 8.159 1.00 43.04 N ATOM 2048 CA ASN C 21 33.313 14.925 6.762 1.00 45.16 C ATOM 2049 CB ASN C 21 33.189 16.438 6.512 1.00 46.62 C ATOM 2050 CG ASN C 21 31.762 16.957 6.721 1.00 49.24 C ATOM 2051 OD1 ASN C 21 30.831 16.593 5.972 1.00 56.70 O ATOM 2052 ND2 ASN C 21 31.582 17.830 7.730 1.00 49.52 N ATOM 2053 C ASN C 21 34.686 14.471 6.266 1.00 45.75 C ATOM 2054 O ASN C 21 35.684 14.670 6.944 1.00 46.28 O ATOM 2055 N CYS C 22 34.723 13.897 5.073 1.00 46.82 N ATOM 2056 CA CYS C 22 35.959 13.487 4.390 1.00 48.35 C ATOM 2057 CB CYS C 22 36.085 11.967 4.403 1.00 49.01 C ATOM 2058 SG CYS C 22 36.404 11.250 6.007 1.00 54.40 S ATOM 2059 C CYS C 22 35.984 13.967 2.918 1.00 47.56 C ATOM 2060 O CYS C 22 34.978 13.866 2.185 1.00 47.67 O ATOM 2061 N VAL C 23 37.123 14.505 2.496 1.00 46.77 N ATOM 2062 CA VAL C 23 37.304 14.992 1.118 1.00 44.55 C ATOM 2063 CB VAL C 23 37.150 16.531 1.002 1.00 44.60 C ATOM 2064 CG1 VAL C 23 37.928 17.212 2.000 1.00 46.21 C ATOM 2065 CG2 VAL C 23 37.482 17.046 −0.374 1.00 41.80 C ATOM 2066 C VAL C 23 38.626 14.498 0.625 1.00 44.64 C ATOM 2067 O VAL C 23 39.675 14.683 1.266 1.00 43.95 O ATOM 2068 N LEU C 24 38.574 13.824 −0.512 1.00 44.47 N ATOM 2069 CA LEU C 24 39.784 13.393 −1.220 1.00 44.52 C ATOM 2070 CB LEU C 24 39.348 12.419 −2.293 1.00 44.25 C ATOM 2071 CG LEU C 24 40.109 11.175 −2.724 1.00 44.73 C ATOM 2072 CD1 LEU C 24 39.957 11.047 −4.204 1.00 40.23 C ATOM 2073 CD2 LEU C 24 41.538 11.066 −2.237 1.00 39.12 C ATOM 2074 C LEU C 24 40.400 14.631 −1.912 1.00 44.53 C ATOM 2075 O LEU C 24 39.900 15.064 −2.955 1.00 44.70 O ATOM 2076 N ARG C 25 41.478 15.178 −1.362 1.00 44.03 N ATOM 2077 CA ARG C 25 42.084 16.424 −1.857 1.00 44.69 C ATOM 2078 CB ARG C 25 42.553 17.314 −0.692 1.00 44.52 C ATOM 2079 CG ARG C 25 41.525 17.578 0.303 1.00 48.32 C ATOM 2080 CD ARG C 25 41.769 18.944 0.893 1.00 55.19 C ATOM 2081 NE ARG C 25 40.566 19.723 0.675 1.00 61.48 N ATOM 2082 CZ ARG C 25 39.708 19.984 1.631 1.00 63.06 C ATOM 2083 NH1 ARG C 25 39.998 19.570 2.840 1.00 64.66 N ATOM 2084 NH2 ARG C 25 38.597 20.665 1.395 1.00 64.06 N ATOM 2085 C ARG C 25 43.299 16.116 −2.694 1.00 44.89 C ATOM 2086 O ARG C 25 43.971 15.093 −2.441 1.00 45.00 O ATOM 2087 N ASP C 26 43.593 17.013 −3.647 1.00 44.78 N ATOM 2088 CA ASP C 26 44.661 16.859 −4.650 1.00 45.57 C ATOM 2089 CB ASP C 26 46.044 17.275 −4.103 1.00 46.72 C ATOM 2090 CG ASP C 26 45.991 18.501 −3.221 1.00 50.19 C ATOM 2091 OD1 ASP C 26 45.405 19.537 −3.629 1.00 53.01 O ATOM 2092 OD2 ASP C 26 46.552 18.429 −2.099 1.00 56.34 O ATOM 2093 C ASP C 26 44.784 15.464 −5.185 1.00 44.38 C ATOM 2094 O ASP C 26 45.871 14.927 −5.215 1.00 43.71 O ATOM 2095 N ALA C 27 43.679 14.845 −5.567 1.00 44.56 N ATOM 2096 CA ALA C 27 43.757 13.530 −6.180 1.00 44.95 C ATOM 2097 CB ALA C 27 42.740 12.552 −5.573 1.00 43.12 C ATOM 2098 C ALA C 27 43.581 13.633 −7.690 1.00 46.25 C ATOM 2099 O ALA C 27 42.797 14.464 −8.174 1.00 46.95 O ATOM 2100 N SER C 28 44.294 12.777 −8.432 1.00 46.99 N ATOM 2101 CA SER C 28 44.153 12.779 −9.869 1.00 48.62 C ATOM 2102 CB SER C 28 45.480 12.479 −10.560 1.00 48.58 C ATOM 2103 OG SER C 28 46.044 11.353 −9.990 1.00 52.33 O ATOM 2104 C SER C 28 43.026 11.836 −10.303 1.00 48.24 C ATOM 2105 O SER C 28 42.716 11.733 −11.473 1.00 49.15 O ATOM 2106 N PHE C 29 42.370 11.220 −9.334 1.00 47.44 N ATOM 2107 CA PHE C 29 41.340 10.221 −9.612 1.00 46.65 C ATOM 2108 CB PHE C 29 41.726 8.894 −8.920 1.00 45.70 C ATOM 2109 CG PHE C 29 43.158 8.502 −9.180 1.00 42.81 C ATOM 2110 CD1 PHE C 29 43.538 8.066 −10.448 1.00 36.25 C ATOM 2111 CE1 PHE C 29 44.850 7.768 −10.742 1.00 40.99 C ATOM 2112 CZ PHE C 29 45.820 7.884 −9.731 1.00 43.75 C ATOM 2113 CE2 PHE C 29 45.441 8.337 −8.441 1.00 40.55 C ATOM 2114 CD2 PHE C 29 44.116 8.649 −8.189 1.00 40.78 C ATOM 2115 C PHE C 29 39.958 10.697 −9.171 1.00 46.58 C ATOM 2116 O PHE C 29 39.831 11.601 −8.317 1.00 46.70 O ATOM 2117 N GLU C 30 38.942 10.067 −9.750 1.00 45.81 N ATOM 2118 CA GLU C 30 37.563 10.269 −9.351 1.00 46.83 C ATOM 2119 CB GLU C 30 36.632 9.980 −10.536 1.00 47.06 C ATOM 2120 CG GLU C 30 36.882 10.950 −11.687 1.00 49.84 C ATOM 2121 CD GLU C 30 36.469 12.382 −11.319 1.00 57.62 C ATOM 2122 OE1 GLU C 30 37.291 13.328 −11.489 1.00 60.20 O ATOM 2123 OE2 GLU C 30 35.322 12.553 −10.835 1.00 58.67 O ATOM 2124 C GLU C 30 37.257 9.401 −8.127 1.00 46.19 C ATOM 2125 O GLU C 30 37.833 8.321 −7.956 1.00 47.70 O ATOM 2126 N LEU C 31 36.387 9.880 −7.259 1.00 45.21 N ATOM 2127 CA LEU C 31 35.899 9.053 −6.142 1.00 44.93 C ATOM 2128 CB LEU C 31 35.102 9.934 −5.217 1.00 43.15 C ATOM 2129 CG LEU C 31 35.111 9.885 −3.699 1.00 44.69 C ATOM 2130 CD1 LEU C 31 33.683 10.296 −3.177 1.00 36.97 C ATOM 2131 CD2 LEU C 31 35.711 8.615 −3.022 1.00 38.29 C ATOM 2132 C LEU C 31 34.937 7.956 −6.652 1.00 45.16 C ATOM 2133 O LEU C 31 33.860 8.246 −7.196 1.00 44.80 O ATOM 2134 N LYS C 32 35.286 6.701 −6.434 1.00 46.15 N ATOM 2135 CA LYS C 32 34.505 5.608 −6.991 1.00 46.54 C ATOM 2136 CB LYS C 32 35.461 4.506 −7.478 1.00 46.96 C ATOM 2137 CG LYS C 32 34.801 3.264 −8.090 1.00 50.13 C ATOM 2138 CD LYS C 32 33.911 3.610 −9.290 1.00 57.71 C ATOM 2139 CE LYS C 32 33.263 2.363 −9.882 1.00 61.56 C ATOM 2140 NZ LYS C 32 33.432 1.172 −8.953 1.00 64.12 N ATOM 2141 C LYS C 32 33.606 5.063 −5.905 1.00 46.00 C ATOM 2142 O LYS C 32 32.462 4.730 −6.158 1.00 46.13 O ATOM 2143 N ASP C 33 34.149 4.969 −4.698 1.00 44.66 N ATOM 2144 CA ASP C 33 33.519 4.229 −3.609 1.00 44.59 C ATOM 2145 CB ASP C 33 33.969 2.787 −3.714 1.00 45.73 C ATOM 2146 CG ASP C 33 32.854 1.826 −3.570 1.00 53.17 C ATOM 2147 OD1 ASP C 33 32.322 1.737 −2.442 1.00 60.90 O ATOM 2148 OD2 ASP C 33 32.510 1.158 −4.597 1.00 61.93 O ATOM 2149 C ASP C 33 34.007 4.777 −2.272 1.00 42.39 C ATOM 2150 O ASP C 33 35.028 5.440 −2.230 1.00 39.76 O ATOM 2151 N THR C 34 33.338 4.398 −1.181 1.00 42.58 N ATOM 2152 CA THR C 34 33.698 4.850 0.198 1.00 43.04 C ATOM 2153 CB THR C 34 32.810 6.031 0.681 1.00 43.33 C ATOM 2154 OG1 THR C 34 31.451 5.618 0.749 1.00 45.15 O ATOM 2155 CG2 THR C 34 32.867 7.227 −0.263 1.00 43.17 C ATOM 2156 C THR C 34 33.529 3.715 1.235 1.00 43.65 C ATOM 2157 O THR C 34 32.668 2.867 1.082 1.00 44.87 O ATOM 2158 N GLY C 35 34.384 3.686 2.256 1.00 43.02 N ATOM 2159 CA GLY C 35 34.214 2.825 3.400 1.00 40.60 C ATOM 2160 C GLY C 35 34.387 3.562 4.711 1.00 40.55 C ATOM 2161 O GLY C 35 35.086 4.603 4.784 1.00 40.16 O ATOM 2162 N TRP C 36 33.817 2.969 5.766 1.00 39.56 N ATOM 2163 CA TRP C 36 33.800 3.546 7.094 1.00 39.04 C ATOM 2164 CB TRP C 36 32.434 4.191 7.420 1.00 37.69 C ATOM 2165 CG TRP C 36 32.204 5.462 6.649 1.00 36.88 C ATOM 2166 CD1 TRP C 36 31.534 5.601 5.445 1.00 37.03 C ATOM 2167 NE1 TRP C 36 31.582 6.905 5.028 1.00 39.08 N ATOM 2168 CE2 TRP C 36 32.299 7.641 5.951 1.00 36.41 C ATOM 2169 CD2 TRP C 36 32.682 6.771 6.993 1.00 35.39 C ATOM 2170 CE3 TRP C 36 33.372 7.289 8.105 1.00 39.61 C ATOM 2171 CZ3 TRP C 36 33.629 8.658 8.149 1.00 41.57 C ATOM 2172 CH2 TRP C 36 33.200 9.514 7.090 1.00 39.46 C ATOM 2173 CZ2 TRP C 36 32.533 9.007 5.998 1.00 38.02 C ATOM 2174 C TRP C 36 34.152 2.464 8.081 1.00 39.80 C ATOM 2175 O TRP C 36 33.630 1.365 7.971 1.00 39.62 O ATOM 2176 N TYR C 37 35.047 2.780 9.028 1.00 39.72 N ATOM 2177 CA TYR C 37 35.586 1.769 9.988 1.00 42.18 C ATOM 2178 CB TYR C 37 37.003 1.298 9.614 1.00 42.50 C ATOM 2179 CG TYR C 37 37.114 0.995 8.128 1.00 46.10 C ATOM 2180 CD1 TYR C 37 36.832 −0.275 7.647 1.00 46.08 C ATOM 2181 CE1 TYR C 37 36.869 −0.558 6.267 1.00 49.05 C ATOM 2182 CZ TYR C 37 37.246 0.447 5.381 1.00 48.62 C ATOM 2183 OH TYR C 37 37.305 0.146 4.032 1.00 51.96 O ATOM 2184 CE2 TYR C 37 37.562 1.732 5.836 1.00 48.05 C ATOM 2185 CD2 TYR C 37 37.495 2.009 7.191 1.00 46.46 C ATOM 2186 C TYR C 37 35.599 2.413 11.358 1.00 41.82 C ATOM 2187 O TYR C 37 35.694 3.624 11.464 1.00 41.95 O ATOM 2188 N ARG C 38 35.544 1.586 12.381 1.00 42.36 N ATOM 2189 CA ARG C 38 35.573 2.021 13.729 1.00 44.49 C ATOM 2190 CB ARG C 38 34.144 2.242 14.237 1.00 43.43 C ATOM 2191 CG ARG C 38 34.110 2.406 15.718 1.00 47.74 C ATOM 2192 CD ARG C 38 32.742 2.530 16.225 1.00 51.14 C ATOM 2193 NE ARG C 38 31.885 1.427 15.821 1.00 52.19 N ATOM 2194 CZ ARG C 38 30.571 1.409 16.035 1.00 57.68 C ATOM 2195 NH1 ARG C 38 29.942 2.452 16.614 1.00 59.02 N ATOM 2196 NH2 ARG C 38 29.868 0.353 15.673 1.00 59.82 N ATOM 2197 C ARG C 38 36.288 0.991 14.613 1.00 45.46 C ATOM 2198 O ARG C 38 36.115 −0.222 14.456 1.00 46.19 O ATOM 2199 N THR C 39 37.083 1.516 15.543 1.00 46.20 N ATOM 2200 CA THR C 39 37.717 0.800 16.641 1.00 46.40 C ATOM 2201 CB THR C 39 39.209 1.155 16.699 1.00 45.51 C ATOM 2202 OG1 THR C 39 39.825 0.817 15.455 1.00 49.49 O ATOM 2203 CG2 THR C 39 39.937 0.406 17.866 1.00 48.80 C ATOM 2204 C THR C 39 36.992 1.338 17.885 1.00 47.15 C ATOM 2205 O THR C 39 37.109 2.523 18.232 1.00 45.10 O ATOM 2206 N LYS C 40 36.167 0.482 18.484 1.00 49.20 N ATOM 2207 CA LYS C 40 35.389 0.844 19.650 1.00 51.33 C ATOM 2208 CB LYS C 40 34.355 −0.221 19.990 1.00 51.30 C ATOM 2209 CG LYS C 40 32.952 0.226 19.595 1.00 55.88 C ATOM 2210 CD LYS C 40 31.926 −0.887 19.626 1.00 59.21 C ATOM 2211 CE LYS C 40 31.099 −0.803 20.895 1.00 63.11 C ATOM 2212 NZ LYS C 40 31.075 −2.176 21.526 1.00 61.59 N ATOM 2213 C LYS C 40 36.333 1.157 20.816 1.00 52.57 C ATOM 2214 O LYS C 40 37.423 0.611 20.886 1.00 50.99 O ATOM 2215 N LEU C 41 35.938 2.114 21.659 1.00 54.39 N ATOM 2216 CA LEU C 41 36.802 2.622 22.737 1.00 57.08 C ATOM 2217 CB LEU C 41 36.066 3.736 23.533 1.00 57.10 C ATOM 2218 CG LEU C 41 36.543 4.136 24.933 1.00 59.84 C ATOM 2219 CD1 LEU C 41 35.549 5.096 25.662 1.00 61.21 C ATOM 2220 CD2 LEU C 41 37.964 4.735 24.863 1.00 62.80 C ATOM 2221 C LEU C 41 37.302 1.465 23.642 1.00 58.11 C ATOM 2222 O LEU C 41 36.505 0.742 24.266 1.00 58.05 O ATOM 2223 N GLY C 42 38.616 1.264 23.669 1.00 59.71 N ATOM 2224 CA GLY C 42 39.187 0.174 24.457 1.00 61.51 C ATOM 2225 C GLY C 42 39.653 −1.023 23.643 1.00 62.72 C ATOM 2226 O GLY C 42 40.460 −1.830 24.139 1.00 63.71 O ATOM 2227 N SER C 43 39.164 −1.138 22.404 1.00 62.76 N ATOM 2228 CA SER C 43 39.511 −2.239 21.519 1.00 62.79 C ATOM 2229 CB SER C 43 38.328 −2.559 20.602 1.00 62.63 C ATOM 2230 OG SER C 43 38.301 −3.927 20.271 1.00 61.87 O ATOM 2231 C SER C 43 40.742 −1.897 20.689 1.00 63.37 C ATOM 2232 O SER C 43 41.116 −0.728 20.557 1.00 63.84 O ATOM 2233 N THR C 44 41.394 −2.912 20.139 1.00 63.50 N ATOM 2234 CA THR C 44 42.377 −2.657 19.070 1.00 64.33 C ATOM 2235 CB THR C 44 43.793 −3.127 19.469 1.00 64.45 C ATOM 2236 OG1 THR C 44 43.781 −4.544 19.687 1.00 66.10 O ATOM 2237 CG2 THR C 44 44.238 −2.424 20.769 1.00 63.59 C ATOM 2238 C THR C 44 41.890 −3.251 17.729 1.00 63.70 C ATOM 2239 O THR C 44 42.568 −3.185 16.695 1.00 64.39 O ATOM 2240 N ASN C 45 40.675 −3.793 17.782 1.00 63.29 N ATOM 2241 CA ASN C 45 39.968 −4.421 16.665 1.00 63.06 C ATOM 2242 CB ASN C 45 38.963 −5.407 17.285 1.00 63.41 C ATOM 2243 CG ASN C 45 38.299 −6.286 16.258 1.00 64.24 C ATOM 2244 OD1 ASN C 45 38.944 −6.744 15.312 1.00 64.63 O ATOM 2245 ND2 ASN C 45 36.996 −6.530 16.436 1.00 64.01 N ATOM 2246 C ASN C 45 39.202 −3.426 15.744 1.00 62.52 C ATOM 2247 O ASN C 45 38.108 −2.951 16.115 1.00 62.14 O ATOM 2248 N GLU C 46 39.763 −3.111 14.573 1.00 61.57 N ATOM 2249 CA GLU C 46 39.080 −2.251 13.572 1.00 61.38 C ATOM 2250 CB GLU C 46 40.062 −1.708 12.530 1.00 61.16 C ATOM 2251 CG GLU C 46 39.403 −1.084 11.308 1.00 63.74 C ATOM 2252 CD GLU C 46 40.014 0.267 10.932 1.00 66.98 C ATOM 2253 OE1 GLU C 46 39.729 1.274 11.635 1.00 69.02 O ATOM 2254 OE2 GLU C 46 40.770 0.320 9.935 1.00 67.74 O ATOM 2255 C GLU C 46 37.917 −2.948 12.868 1.00 60.84 C ATOM 2256 O GLU C 46 38.086 −4.018 12.322 1.00 61.63 O ATOM 2257 N GLN C 47 36.748 −2.322 12.856 1.00 60.18 N ATOM 2258 CA GLN C 47 35.542 −2.929 12.279 1.00 59.69 C ATOM 2259 CB GLN C 47 34.492 −3.142 13.364 1.00 60.04 C ATOM 2260 CG GLN C 47 34.685 −4.423 14.153 1.00 63.45 C ATOM 2261 CD GLN C 47 33.988 −4.364 15.502 1.00 67.03 C ATOM 2262 OE1 GLN C 47 33.722 −5.409 16.101 1.00 69.04 O ATOM 2263 NE2 GLN C 47 33.687 −3.134 15.992 1.00 65.48 N ATOM 2264 C GLN C 47 34.882 −2.103 11.188 1.00 57.90 C ATOM 2265 O GLN C 47 34.807 −0.893 11.276 1.00 56.91 O ATOM 2266 N SER C 48 34.333 −2.792 10.205 1.00 57.17 N ATOM 2267 CA SER C 48 33.545 −2.155 9.151 1.00 57.02 C ATOM 2268 CB SER C 48 33.367 −3.095 7.949 1.00 57.30 C ATOM 2269 OG SER C 48 33.469 −2.341 6.749 1.00 59.39 O ATOM 2270 C SER C 48 32.203 −1.664 9.682 1.00 55.73 C ATOM 2271 O SER C 48 31.564 −2.325 10.497 1.00 55.50 O ATOM 2272 N ILE C 49 31.823 −0.460 9.257 1.00 55.13 N ATOM 2273 CA ILE C 49 30.555 0.176 9.651 1.00 54.08 C ATOM 2274 CB ILE C 49 30.701 1.702 9.867 1.00 53.11 C ATOM 2275 CG1 ILE C 49 31.364 2.013 11.191 1.00 54.19 C ATOM 2276 CD1 ILE C 49 31.747 3.486 11.251 1.00 50.86 C ATOM 2277 CG2 ILE C 49 29.335 2.437 9.866 1.00 53.88 C ATOM 2278 C ILE C 49 29.495 −0.094 8.577 1.00 53.70 C ATOM 2279 O ILE C 49 29.695 0.176 7.389 1.00 54.09 O ATOM 2280 N SER C 50 28.372 −0.637 9.027 1.00 53.80 N ATOM 2281 CA SER C 50 27.170 −0.832 8.215 1.00 53.15 C ATOM 2282 CB SER C 50 26.378 −2.049 8.731 1.00 53.47 C ATOM 2283 OG SER C 50 27.216 −3.191 8.674 1.00 55.46 O ATOM 2284 C SER C 50 26.299 0.421 8.248 1.00 51.25 C ATOM 2285 O SER C 50 25.876 0.861 9.314 1.00 50.95 O ATOM 2286 N ILE C 51 26.055 0.964 7.058 1.00 49.62 N ATOM 2287 CA ILE C 51 25.252 2.177 6.854 1.00 47.96 C ATOM 2288 CB ILE C 51 25.704 2.918 5.527 1.00 47.87 C ATOM 2289 CG1 ILE C 51 27.198 3.362 5.611 1.00 47.14 C ATOM 2290 CD1 ILE C 51 27.596 4.066 6.953 1.00 42.36 C ATOM 2291 CG2 ILE C 51 24.764 4.088 5.185 1.00 47.30 C ATOM 2292 C ILE C 51 23.750 1.837 6.844 1.00 46.21 C ATOM 2293 O ILE C 51 23.318 0.974 6.084 1.00 47.08 O ATOM 2294 N GLY C 52 22.958 2.488 7.697 1.00 44.14 N ATOM 2295 CA GLY C 52 21.505 2.239 7.784 1.00 41.65 C ATOM 2296 C GLY C 52 21.099 2.653 9.184 1.00 40.74 C ATOM 2297 O GLY C 52 21.943 2.713 10.069 1.00 40.48 O ATOM 2298 N GLY C 53 19.822 2.961 9.391 1.00 38.99 N ATOM 2299 CA GLY C 53 19.345 3.387 10.677 1.00 37.19 C ATOM 2300 C GLY C 53 19.888 4.738 11.055 1.00 37.85 C ATOM 2301 O GLY C 53 19.829 5.692 10.269 1.00 37.66 O ATOM 2302 N ARG C 54 20.424 4.812 12.277 1.00 38.16 N ATOM 2303 CA ARG C 54 21.107 5.990 12.806 1.00 36.67 C ATOM 2304 CB ARG C 54 21.487 5.783 14.286 1.00 37.09 C ATOM 2305 CG ARG C 54 20.294 5.610 15.167 1.00 36.01 C ATOM 2306 CD ARG C 54 20.611 5.607 16.667 1.00 37.36 C ATOM 2307 NE ARG C 54 21.596 4.563 16.963 1.00 39.11 N ATOM 2308 CZ ARG C 54 22.885 4.774 17.227 1.00 39.90 C ATOM 2309 NH1 ARG C 54 23.418 6.002 17.263 1.00 35.96 N ATOM 2310 NH2 ARG C 54 23.645 3.734 17.490 1.00 38.73 N ATOM 2311 C ARG C 54 22.310 6.430 12.016 1.00 37.64 C ATOM 2312 O ARG C 54 22.696 7.611 12.105 1.00 38.33 O ATOM 2313 N TYR C 55 22.927 5.527 11.242 1.00 38.47 N ATOM 2314 CA TYR C 55 24.111 5.852 10.435 1.00 38.95 C ATOM 2315 CB TYR C 55 25.104 4.647 10.444 1.00 41.10 C ATOM 2316 CG TYR C 55 25.676 4.328 11.842 1.00 43.73 C ATOM 2317 CD1 TYR C 55 24.897 3.737 12.850 1.00 45.50 C ATOM 2318 CE1 TYR C 55 25.432 3.473 14.108 1.00 47.29 C ATOM 2319 CZ TYR C 55 26.778 3.788 14.349 1.00 47.61 C ATOM 2320 OH TYR C 55 27.392 3.558 15.581 1.00 49.34 O ATOM 2321 CE2 TYR C 55 27.541 4.359 13.367 1.00 44.66 C ATOM 2322 CD2 TYR C 55 27.001 4.622 12.141 1.00 44.65 C ATOM 2323 C TYR C 55 23.703 6.228 8.973 1.00 38.22 C ATOM 2324 O TYR C 55 23.137 5.426 8.270 1.00 38.89 O ATOM 2325 N VAL C 56 24.009 7.436 8.522 1.00 37.84 N ATOM 2326 CA VAL C 56 23.618 7.965 7.202 1.00 37.02 C ATOM 2327 CB VAL C 56 22.603 9.173 7.358 1.00 37.86 C ATOM 2328 CG1 VAL C 56 22.116 9.728 5.981 1.00 36.06 C ATOM 2329 CG2 VAL C 56 21.430 8.757 8.169 1.00 36.23 C ATOM 2330 C VAL C 56 24.901 8.476 6.531 1.00 38.69 C ATOM 2331 O VAL C 56 25.605 9.334 7.094 1.00 37.27 O ATOM 2332 N GLU C 57 25.230 7.898 5.369 1.00 39.95 N ATOM 2333 CA GLU C 57 26.318 8.383 4.518 1.00 41.91 C ATOM 2334 CB GLU C 57 27.001 7.223 3.793 1.00 42.73 C ATOM 2335 CG GLU C 57 28.243 7.712 3.058 1.00 44.86 C ATOM 2336 CD GLU C 57 29.213 6.641 2.626 1.00 46.27 C ATOM 2337 OE1 GLU C 57 30.406 6.928 2.665 1.00 51.32 O ATOM 2338 OE2 GLU C 57 28.819 5.529 2.281 1.00 45.88 O ATOM 2339 C GLU C 57 25.772 9.321 3.461 1.00 42.24 C ATOM 2340 O GLU C 57 24.679 9.095 2.933 1.00 42.46 O ATOM 2341 N THR C 58 26.505 10.370 3.128 1.00 42.56 N ATOM 2342 CA THR C 58 26.114 11.189 1.984 1.00 44.27 C ATOM 2343 CB THR C 58 25.754 12.622 2.431 1.00 45.63 C ATOM 2344 OG1 THR C 58 24.690 12.556 3.388 1.00 44.93 O ATOM 2345 CG2 THR C 58 25.232 13.504 1.208 1.00 46.97 C ATOM 2346 C THR C 58 27.348 11.189 1.130 1.00 44.50 C ATOM 2347 O THR C 58 28.413 11.350 1.666 1.00 43.33 O ATOM 2348 N VAL C 59 27.230 10.942 −0.176 1.00 45.04 N ATOM 2349 CA VAL C 59 28.406 10.977 −1.063 1.00 45.53 C ATOM 2350 CB VAL C 59 28.708 9.588 −1.708 1.00 46.05 C ATOM 2351 CG1 VAL C 59 29.915 9.649 −2.706 1.00 47.53 C ATOM 2352 CG2 VAL C 59 29.006 8.579 −0.643 1.00 45.51 C ATOM 2353 C VAL C 59 28.206 12.053 −2.134 1.00 45.35 C ATOM 2354 O VAL C 59 27.147 12.120 −2.743 1.00 44.02 O ATOM 2355 N ASN C 60 29.203 12.919 −2.317 1.00 44.36 N ATOM 2356 CA ASN C 60 29.194 13.869 −3.435 1.00 44.75 C ATOM 2357 CB ASN C 60 29.177 15.316 −2.912 1.00 45.64 C ATOM 2358 CG ASN C 60 28.884 16.325 −4.015 1.00 47.39 C ATOM 2359 OD1 ASN C 60 29.294 16.141 −5.154 1.00 49.89 O ATOM 2360 ND2 ASN C 60 28.148 17.385 −3.681 1.00 49.11 N ATOM 2361 C ASN C 60 30.404 13.658 −4.329 1.00 44.46 C ATOM 2362 O ASN C 60 31.482 14.175 −4.051 1.00 44.94 O ATOM 2363 N LYS C 61 30.277 12.837 −5.357 1.00 43.78 N ATOM 2364 CA LYS C 61 31.416 12.530 −6.207 1.00 43.85 C ATOM 2365 CB LYS C 61 31.024 11.439 −7.200 1.00 45.23 C ATOM 2366 CG LYS C 61 30.890 10.014 −6.579 1.00 46.82 C ATOM 2367 CD LYS C 61 30.106 9.171 −7.582 1.00 50.75 C ATOM 2368 CE LYS C 61 29.705 7.801 −7.064 1.00 54.46 C ATOM 2369 NZ LYS C 61 30.794 6.802 −7.151 1.00 54.88 N ATOM 2370 C LYS C 61 31.910 13.801 −6.932 1.00 43.81 C ATOM 2371 O LYS C 61 33.080 13.971 −7.175 1.00 42.45 O ATOM 2372 N GLY C 62 31.000 14.714 −7.249 1.00 44.61 N ATOM 2373 CA GLY C 62 31.383 15.991 −7.859 1.00 45.46 C ATOM 2374 C GLY C 62 32.487 16.728 −7.119 1.00 45.37 C ATOM 2375 O GLY C 62 33.376 17.295 −7.727 1.00 45.73 O ATOM 2376 N SER C 63 32.450 16.704 −5.792 1.00 45.46 N ATOM 2377 CA SER C 63 33.420 17.441 −5.008 1.00 44.70 C ATOM 2378 CB SER C 63 32.688 18.416 −4.091 1.00 45.19 C ATOM 2379 OG SER C 63 31.893 17.677 −3.181 1.00 47.62 O ATOM 2380 C SER C 63 34.264 16.451 −4.232 1.00 44.60 C ATOM 2381 O SER C 63 34.979 16.823 −3.314 1.00 45.58 O ATOM 2382 N LYS C 64 34.200 15.185 −4.631 1.00 43.31 N ATOM 2383 CA LYS C 64 34.998 14.106 −4.028 1.00 42.72 C ATOM 2384 CB LYS C 64 36.477 14.180 −4.442 1.00 43.43 C ATOM 2385 CG LYS C 64 36.775 14.385 −5.937 1.00 42.33 C ATOM 2386 CD LYS C 64 38.280 14.079 −6.230 1.00 41.50 C ATOM 2387 CE LYS C 64 38.590 14.577 −7.695 1.00 39.78 C ATOM 2388 NZ LYS C 64 39.915 14.109 −8.180 1.00 42.69 N ATOM 2389 C LYS C 64 34.886 14.092 −2.496 1.00 43.21 C ATOM 2390 O LYS C 64 35.878 13.779 −1.795 1.00 42.92 O ATOM 2391 N SER C 65 33.699 14.441 −1.992 1.00 41.43 N ATOM 2392 CA SER C 65 33.469 14.458 −0.580 1.00 42.62 C ATOM 2393 CB SER C 65 33.231 15.866 −0.083 1.00 43.83 C ATOM 2394 OG SER C 65 32.354 16.529 −0.959 1.00 45.50 O ATOM 2395 C SER C 65 32.347 13.565 −0.135 1.00 42.45 C ATOM 2396 O SER C 65 31.421 13.224 −0.874 1.00 40.59 O ATOM 2397 N PHE C 66 32.466 13.139 1.103 1.00 42.45 N ATOM 2398 CA PHE C 66 31.473 12.198 1.636 1.00 43.16 C ATOM 2399 CB PHE C 66 31.730 10.756 1.181 1.00 42.27 C ATOM 2400 CG PHE C 66 33.099 10.222 1.510 1.00 44.09 C ATOM 2401 CD1 PHE C 66 34.242 10.716 0.857 1.00 42.19 C ATOM 2402 CE1 PHE C 66 35.517 10.219 1.123 1.00 44.28 C ATOM 2403 CZ PHE C 66 35.670 9.175 2.052 1.00 45.40 C ATOM 2404 CE2 PHE C 66 34.513 8.620 2.721 1.00 43.80 C ATOM 2405 CD2 PHE C 66 33.244 9.152 2.449 1.00 46.12 C ATOM 2406 C PHE C 66 31.421 12.354 3.123 1.00 43.16 C ATOM 2407 O PHE C 66 32.351 12.914 3.730 1.00 43.47 O ATOM 2408 N SER C 67 30.295 12.004 3.716 1.00 43.08 N ATOM 2409 CA SER C 67 30.192 12.283 5.145 1.00 43.78 C ATOM 2410 CB SER C 67 29.498 13.599 5.348 1.00 42.88 C ATOM 2411 OG SER C 67 28.148 13.307 5.122 1.00 50.83 O ATOM 2412 C SER C 67 29.420 11.172 5.783 1.00 42.30 C ATOM 2413 O SER C 67 28.653 10.502 5.119 1.00 42.27 O ATOM 2414 N LEU C 68 29.704 10.935 7.050 1.00 40.76 N ATOM 2415 CA LEU C 68 28.938 10.035 7.877 1.00 39.22 C ATOM 2416 CB LEU C 68 29.870 9.117 8.675 1.00 39.26 C ATOM 2417 CG LEU C 68 29.519 7.673 9.067 1.00 39.79 C ATOM 2418 CD1 LEU C 68 30.187 7.273 10.332 1.00 36.92 C ATOM 2419 CD2 LEU C 68 28.064 7.184 8.998 1.00 41.23 C ATOM 2420 C LEU C 68 28.281 10.919 8.932 1.00 38.92 C ATOM 2421 O LEU C 68 28.962 11.636 9.668 1.00 36.62 O ATOM 2422 N ARG C 69 26.988 10.734 9.088 1.00 38.05 N ATOM 2423 CA ARG C 69 26.216 11.297 10.182 1.00 38.81 C ATOM 2424 CB ARG C 69 24.957 12.018 9.603 1.00 37.83 C ATOM 2425 CG ARG C 69 24.394 12.996 10.666 1.00 42.79 C ATOM 2426 CD ARG C 69 23.175 13.730 10.200 1.00 53.15 C ATOM 2427 NE ARG C 69 23.050 14.889 11.076 1.00 60.64 N ATOM 2428 CZ ARG C 69 22.234 14.973 12.136 1.00 64.79 C ATOM 2429 NH1 ARG C 69 21.415 13.954 12.452 1.00 64.71 N ATOM 2430 NH2 ARG C 69 22.227 16.089 12.882 1.00 64.93 N ATOM 2431 C ARG C 69 25.714 10.174 11.063 1.00 38.49 C ATOM 2432 O ARG C 69 25.016 9.296 10.576 1.00 38.05 O ATOM 2433 N ILE C 70 26.036 10.204 12.355 1.00 38.71 N ATOM 2434 CA ILE C 70 25.420 9.290 13.321 1.00 38.97 C ATOM 2435 CB ILE C 70 26.478 8.582 14.218 1.00 39.33 C ATOM 2436 CG1 ILE C 70 27.623 8.001 13.370 1.00 41.07 C ATOM 2437 CD1 ILE C 70 28.826 7.749 14.203 1.00 42.56 C ATOM 2438 CG2 ILE C 70 25.853 7.519 15.050 1.00 36.50 C ATOM 2439 C ILE C 70 24.425 10.106 14.188 1.00 38.51 C ATOM 2440 O ILE C 70 24.863 10.970 14.928 1.00 38.32 O ATOM 2441 N SER C 71 23.124 9.833 14.069 1.00 36.88 N ATOM 2442 CA SER C 71 22.084 10.437 14.955 1.00 38.63 C ATOM 2443 CB SER C 71 20.691 10.355 14.353 1.00 36.29 C ATOM 2444 OG SER C 71 20.721 10.830 13.058 1.00 42.47 O ATOM 2445 C SER C 71 21.938 9.783 16.308 1.00 37.24 C ATOM 2446 O SER C 71 22.280 8.640 16.509 1.00 39.57 O ATOM 2447 N ASP C 72 21.394 10.530 17.218 1.00 37.94 N ATOM 2448 CA ASP C 72 21.064 10.056 18.525 1.00 38.88 C ATOM 2449 CB ASP C 72 19.761 9.261 18.465 1.00 38.48 C ATOM 2450 CG ASP C 72 19.127 9.150 19.805 1.00 40.88 C ATOM 2451 OD1 ASP C 72 19.397 10.036 20.649 1.00 41.95 O ATOM 2452 OD2 ASP C 72 18.355 8.204 20.029 1.00 46.35 O ATOM 2453 C ASP C 72 22.192 9.248 19.194 1.00 39.02 C ATOM 2454 O ASP C 72 21.996 8.088 19.548 1.00 40.28 O ATOM 2455 N LEU C 73 23.354 9.857 19.369 1.00 38.81 N ATOM 2456 CA LEU C 73 24.525 9.137 19.900 1.00 39.26 C ATOM 2457 CB LEU C 73 25.754 10.076 20.004 1.00 38.40 C ATOM 2458 CG LEU C 73 26.271 10.505 18.635 1.00 37.52 C ATOM 2459 CD1 LEU C 73 27.086 11.766 18.820 1.00 36.13 C ATOM 2460 CD2 LEU C 73 27.118 9.367 18.077 1.00 35.66 C ATOM 2461 C LEU C 73 24.290 8.464 21.258 1.00 38.78 C ATOM 2462 O LEU C 73 23.600 9.018 22.132 1.00 38.58 O ATOM 2463 N ARG C 74 24.851 7.275 21.430 1.00 38.74 N ATOM 2464 CA ARG C 74 24.881 6.575 22.744 1.00 40.73 C ATOM 2465 CB ARG C 74 24.123 5.247 22.684 1.00 40.63 C ATOM 2466 CG ARG C 74 23.674 4.750 21.330 1.00 44.45 C ATOM 2467 CD ARG C 74 22.291 5.411 21.028 1.00 52.00 C ATOM 2468 NE ARG C 74 21.296 4.424 20.582 1.00 57.73 N ATOM 2469 CZ ARG C 74 20.034 4.701 20.272 1.00 54.39 C ATOM 2470 NH1 ARG C 74 19.236 3.719 19.917 1.00 55.75 N ATOM 2471 NH2 ARG C 74 19.588 5.942 20.292 1.00 49.28 N ATOM 2472 C ARG C 74 26.351 6.305 23.159 1.00 41.08 C ATOM 2473 O ARG C 74 27.223 6.297 22.283 1.00 39.54 O ATOM 2474 N VAL C 75 26.629 6.061 24.453 1.00 41.83 N ATOM 2475 CA VAL C 75 28.019 5.793 24.874 1.00 42.82 C ATOM 2476 CB VAL C 75 28.167 5.434 26.383 1.00 42.84 C ATOM 2477 CG1 VAL C 75 27.517 6.484 27.263 1.00 42.05 C ATOM 2478 CG2 VAL C 75 27.552 4.094 26.683 1.00 44.76 C ATOM 2479 C VAL C 75 28.658 4.705 24.017 1.00 43.85 C ATOM 2480 O VAL C 75 29.833 4.797 23.665 1.00 44.32 O ATOM 2481 N GLU C 76 27.888 3.668 23.662 1.00 44.43 N ATOM 2482 CA GLU C 76 28.437 2.562 22.865 1.00 45.15 C ATOM 2483 CB GLU C 76 27.474 1.346 22.799 1.00 46.21 C ATOM 2484 CG GLU C 76 25.983 1.699 22.474 1.00 51.67 C ATOM 2485 CD GLU C 76 25.070 1.966 23.696 1.00 56.22 C ATOM 2486 OE1 GLU C 76 23.911 1.494 23.654 1.00 60.97 O ATOM 2487 OE2 GLU C 76 25.456 2.651 24.684 1.00 58.26 O ATOM 2488 C GLU C 76 28.927 3.022 21.474 1.00 44.53 C ATOM 2489 O GLU C 76 29.708 2.291 20.812 1.00 43.93 O ATOM 2490 N ASP C 77 28.535 4.236 21.040 1.00 42.84 N ATOM 2491 CA ASP C 77 29.055 4.766 19.743 1.00 41.95 C ATOM 2492 CB ASP C 77 28.118 5.832 19.168 1.00 42.62 C ATOM 2493 CG ASP C 77 26.752 5.282 18.781 1.00 45.69 C ATOM 2494 OD1 ASP C 77 26.657 4.110 18.318 1.00 43.73 O ATOM 2495 OD2 ASP C 77 25.773 6.049 18.913 1.00 44.99 O ATOM 2496 C ASP C 77 30.508 5.313 19.846 1.00 40.76 C ATOM 2497 O ASP C 77 31.127 5.640 18.846 1.00 40.30 O ATOM 2498 N SER C 78 31.024 5.464 21.061 1.00 40.14 N ATOM 2499 CA SER C 78 32.383 5.978 21.240 1.00 40.43 C ATOM 2500 CB SER C 78 32.751 6.039 22.716 1.00 38.77 C ATOM 2501 OG SER C 78 31.800 6.795 23.385 1.00 40.31 O ATOM 2502 C SER C 78 33.411 5.118 20.519 1.00 40.44 C ATOM 2503 O SER C 78 33.259 3.898 20.413 1.00 41.58 O ATOM 2504 N GLY C 79 34.456 5.763 20.014 1.00 39.91 N ATOM 2505 CA GLY C 79 35.569 5.065 19.403 1.00 39.20 C ATOM 2506 C GLY C 79 36.243 5.931 18.378 1.00 39.12 C ATOM 2507 O GLY C 79 35.911 7.103 18.272 1.00 38.52 O ATOM 2508 N THR C 80 37.125 5.335 17.584 1.00 39.32 N ATOM 2509 CA THR C 80 37.814 6.062 16.539 1.00 40.74 C ATOM 2510 CB THR C 80 39.345 5.858 16.627 1.00 40.22 C ATOM 2511 OG1 THR C 80 39.806 6.345 17.896 1.00 41.93 O ATOM 2512 CG2 THR C 80 40.088 6.585 15.475 1.00 39.67 C ATOM 2513 C THR C 80 37.331 5.592 15.192 1.00 41.67 C ATOM 2514 O THR C 80 37.464 4.406 14.867 1.00 42.93 O ATOM 2515 N TYR C 81 36.797 6.532 14.413 1.00 41.16 N ATOM 2516 CA TYR C 81 36.235 6.302 13.098 1.00 41.38 C ATOM 2517 CB TYR C 81 34.934 7.118 12.928 1.00 41.71 C ATOM 2518 CG TYR C 81 33.832 6.627 13.831 1.00 41.50 C ATOM 2519 CD1 TYR C 81 32.840 5.753 13.343 1.00 42.16 C ATOM 2520 CE1 TYR C 81 31.777 5.275 14.208 1.00 37.37 C ATOM 2521 CZ TYR C 81 31.752 5.716 15.516 1.00 42.71 C ATOM 2522 OH TYR C 81 30.763 5.238 16.353 1.00 44.53 O ATOM 2523 CE2 TYR C 81 32.747 6.575 16.023 1.00 41.06 C ATOM 2524 CD2 TYR C 81 33.763 7.031 15.181 1.00 40.89 C ATOM 2525 C TYR C 81 37.221 6.760 12.031 1.00 41.95 C ATOM 2526 O TYR C 81 37.878 7.771 12.247 1.00 42.20 O ATOM 2527 N LYS C 82 37.373 5.968 10.947 1.00 41.37 N ATOM 2528 CA LYS C 82 38.121 6.382 9.764 1.00 42.18 C ATOM 2529 CB LYS C 82 39.448 5.632 9.579 1.00 41.37 C ATOM 2530 CG LYS C 82 40.368 5.886 10.712 1.00 46.60 C ATOM 2531 CD LYS C 82 41.821 5.742 10.339 1.00 52.93 C ATOM 2532 CE LYS C 82 42.613 5.556 11.625 1.00 55.71 C ATOM 2533 NZ LYS C 82 44.075 5.483 11.354 1.00 61.02 N ATOM 2534 C LYS C 82 37.281 6.164 8.540 1.00 41.18 C ATOM 2535 O LYS C 82 36.568 5.188 8.473 1.00 40.69 O ATOM 2536 N CYS C 83 37.420 7.065 7.587 1.00 40.93 N ATOM 2537 CA CYS C 83 36.864 6.904 6.294 1.00 44.17 C ATOM 2538 CB CYS C 83 36.274 8.199 5.799 1.00 43.61 C ATOM 2539 SG CYS C 83 37.465 9.490 5.676 1.00 48.89 S ATOM 2540 C CYS C 83 37.964 6.491 5.319 1.00 45.48 C ATOM 2541 O CYS C 83 39.145 6.776 5.525 1.00 46.68 O ATOM 2542 N GLN C 84 37.567 5.801 4.258 1.00 45.72 N ATOM 2543 CA GLN C 84 38.485 5.529 3.193 1.00 44.76 C ATOM 2544 CB GLN C 84 38.975 4.074 3.282 1.00 44.52 C ATOM 2545 CG GLN C 84 39.885 3.726 2.122 1.00 45.70 C ATOM 2546 CD GLN C 84 40.912 2.652 2.388 1.00 49.09 C ATOM 2547 OE1 GLN C 84 42.083 2.752 1.918 1.00 52.22 O ATOM 2548 NE2 GLN C 84 40.512 1.628 3.106 1.00 43.81 N ATOM 2549 C GLN C 84 37.809 5.818 1.886 1.00 44.70 C ATOM 2550 O GLN C 84 36.677 5.362 1.628 1.00 45.18 O ATOM 2551 N ALA C 85 38.503 6.588 1.058 1.00 44.54 N ATOM 2552 CA ALA C 85 38.073 6.857 −0.324 1.00 43.12 C ATOM 2553 CB ALA C 85 38.450 8.228 −0.717 1.00 41.23 C ATOM 2554 C ALA C 85 38.750 5.826 −1.261 1.00 43.54 C ATOM 2555 O ALA C 85 40.001 5.667 −1.262 1.00 42.69 O ATOM 2556 N PHE C 86 37.919 5.123 −2.014 1.00 42.31 N ATOM 2557 CA PHE C 86 38.354 4.226 −3.079 1.00 42.97 C ATOM 2558 CB PHE C 86 37.549 2.932 −3.061 1.00 43.29 C ATOM 2559 CG PHE C 86 37.713 2.185 −1.762 1.00 45.80 C ATOM 2560 CD1 PHE C 86 36.695 2.201 −0.782 1.00 42.22 C ATOM 2561 CE1 PHE C 86 36.905 1.563 0.421 1.00 42.36 C ATOM 2562 CZ PHE C 86 38.101 0.899 0.668 1.00 42.36 C ATOM 2563 CE2 PHE C 86 39.105 0.869 −0.301 1.00 42.11 C ATOM 2564 CD2 PHE C 86 38.913 1.529 −1.489 1.00 43.32 C ATOM 2565 C PHE C 86 38.206 4.860 −4.425 1.00 42.06 C ATOM 2566 O PHE C 86 37.274 5.618 −4.692 1.00 41.81 O ATOM 2567 N TYR C 87 39.169 4.558 −5.277 1.00 42.72 N ATOM 2568 CA TYR C 87 39.184 5.052 −6.646 1.00 42.08 C ATOM 2569 CB TYR C 87 39.938 6.398 −6.719 1.00 43.64 C ATOM 2570 CG TYR C 87 41.182 6.458 −5.859 1.00 44.34 C ATOM 2571 CD1 TYR C 87 41.161 7.043 −4.589 1.00 46.58 C ATOM 2572 CE1 TYR C 87 42.332 7.098 −3.787 1.00 46.11 C ATOM 2573 CZ TYR C 87 43.502 6.541 −4.268 1.00 47.59 C ATOM 2574 OH TYR C 87 44.668 6.553 −3.504 1.00 48.00 O ATOM 2575 CE2 TYR C 87 43.538 5.961 −5.531 1.00 47.66 C ATOM 2576 CD2 TYR C 87 42.385 5.926 −6.320 1.00 48.34 C ATOM 2577 C TYR C 87 39.850 3.971 −7.494 1.00 41.63 C ATOM 2578 O TYR C 87 40.505 3.080 −6.962 1.00 40.18 O ATOM 2579 N VAL C 88 39.649 4.060 −8.807 1.00 40.58 N ATOM 2580 CA VAL C 88 40.190 3.116 −9.791 1.00 38.74 C ATOM 2581 CB VAL C 88 39.090 2.177 −10.417 1.00 38.40 C ATOM 2582 CG1 VAL C 88 38.522 1.217 −9.367 1.00 35.07 C ATOM 2583 CG2 VAL C 88 37.906 2.991 −11.012 1.00 37.81 C ATOM 2584 C VAL C 88 40.912 3.876 −10.888 1.00 38.92 C ATOM 2585 O VAL C 88 40.597 5.063 −11.145 1.00 38.50 O ATOM 2586 N PHE C 89 41.883 3.200 −11.534 1.00 37.31 N ATOM 2587 CA PHE C 89 42.656 3.790 −12.610 1.00 36.15 C ATOM 2588 CB PHE C 89 43.787 4.711 −12.062 1.00 36.75 C ATOM 2589 CG PHE C 89 44.555 4.132 −10.846 1.00 36.77 C ATOM 2590 CD1 PHE C 89 44.066 4.284 −9.550 1.00 38.64 C ATOM 2591 CE1 PHE C 89 44.743 3.751 −8.429 1.00 36.48 C ATOM 2592 CZ PHE C 89 45.932 3.067 −8.631 1.00 39.07 C ATOM 2593 CE2 PHE C 89 46.401 2.894 −9.914 1.00 37.47 C ATOM 2594 CD2 PHE C 89 45.720 3.431 −11.009 1.00 35.24 C ATOM 2595 C PHE C 89 43.291 2.637 −13.345 1.00 37.04 C ATOM 2596 O PHE C 89 43.464 1.544 −12.808 1.00 34.79 O ATOM 2597 N PHE C 90 43.645 2.885 −14.591 1.00 36.52 N ATOM 2598 CA PHE C 90 44.378 1.903 −15.331 1.00 37.25 C ATOM 2599 CB PHE C 90 44.357 2.209 −16.812 1.00 36.55 C ATOM 2600 CG PHE C 90 43.017 1.968 −17.458 1.00 35.98 C ATOM 2601 CD1 PHE C 90 42.555 0.662 −17.653 1.00 37.27 C ATOM 2602 CE1 PHE C 90 41.365 0.403 −18.313 1.00 35.06 C ATOM 2603 CZ PHE C 90 40.588 1.508 −18.772 1.00 40.72 C ATOM 2604 CE2 PHE C 90 41.050 2.842 −18.572 1.00 35.96 C ATOM 2605 CD2 PHE C 90 42.266 3.045 −17.941 1.00 30.26 C ATOM 2606 C PHE C 90 45.793 1.765 −14.824 1.00 38.44 C ATOM 2607 O PHE C 90 46.373 2.754 −14.304 1.00 37.09 O ATOM 2608 N ALA C 91 46.305 0.523 −14.949 1.00 38.72 N ATOM 2609 CA ALA C 91 47.654 0.146 −14.505 1.00 40.42 C ATOM 2610 CB ALA C 91 47.942 −1.248 −14.918 1.00 39.03 C ATOM 2611 C ALA C 91 48.790 1.067 −14.986 1.00 41.68 C ATOM 2612 O ALA C 91 49.730 1.312 −14.221 1.00 42.62 O ATOM 2613 N GLU C 92 48.683 1.578 −16.211 1.00 42.40 N ATOM 2614 CA GLU C 92 49.667 2.488 −16.825 1.00 45.96 C ATOM 2615 CB GLU C 92 49.609 2.365 −18.350 1.00 46.83 C ATOM 2616 CG GLU C 92 49.960 0.958 −18.882 1.00 54.78 C ATOM 2617 CD GLU C 92 51.461 0.705 −19.228 1.00 65.73 C ATOM 2618 OE1 GLU C 92 51.753 0.838 −20.455 1.00 68.70 O ATOM 2619 OE2 GLU C 92 52.324 0.333 −18.328 1.00 67.00 O ATOM 2620 C GLU C 92 49.561 3.991 −16.450 1.00 46.75 C ATOM 2621 O GLU C 92 50.310 4.807 −16.965 1.00 47.85 O ATOM 2622 N ASP C 93 48.622 4.360 −15.586 1.00 46.84 N ATOM 2623 CA ASP C 93 48.578 5.692 −14.997 1.00 47.98 C ATOM 2624 CB ASP C 93 47.402 5.780 −14.024 1.00 48.91 C ATOM 2625 CG ASP C 93 47.048 7.201 −13.702 1.00 53.37 C ATOM 2626 OD1 ASP C 93 47.669 7.763 −12.756 1.00 59.02 O ATOM 2627 OD2 ASP C 93 46.171 7.745 −14.411 1.00 52.66 O ATOM 2628 C ASP C 93 49.855 5.869 −14.185 1.00 46.99 C ATOM 2629 O ASP C 93 50.113 5.046 −13.293 1.00 48.62 O ATOM 2630 N VAL C 94 50.638 6.908 −14.499 1.00 43.77 N ATOM 2631 CA VAL C 94 51.934 7.192 −13.906 1.00 40.69 C ATOM 2632 CB VAL C 94 53.120 6.915 −14.893 1.00 40.79 C ATOM 2633 CG1 VAL C 94 52.921 7.686 −16.247 1.00 38.04 C ATOM 2634 CG2 VAL C 94 53.260 5.446 −15.184 1.00 38.24 C ATOM 2635 C VAL C 94 51.966 8.674 −13.471 1.00 40.53 C ATOM 2636 O VAL C 94 51.209 9.479 −13.973 1.00 39.56 O ATOM 2637 N GLY C 95 52.867 9.022 −12.553 1.00 40.49 N ATOM 2638 CA GLY C 95 53.050 10.415 −12.093 1.00 38.78 C ATOM 2639 C GLY C 95 52.272 10.847 −10.852 1.00 38.81 C ATOM 2640 O GLY C 95 52.535 11.890 −10.335 1.00 40.05 O ATOM 2641 N SER C 96 51.312 10.069 −10.362 1.00 37.58 N ATOM 2642 CA SER C 96 50.546 10.497 −9.227 1.00 39.65 C ATOM 2643 CB SER C 96 49.053 10.780 −9.608 1.00 39.56 C ATOM 2644 OG SER C 96 49.035 11.894 −10.504 1.00 43.48 O ATOM 2645 C SER C 96 50.567 9.465 −8.136 1.00 39.35 C ATOM 2646 O SER C 96 50.517 8.279 −8.401 1.00 39.38 O ATOM 2647 N ASN C 97 50.640 9.963 −6.915 1.00 39.49 N ATOM 2648 CA ASN C 97 50.421 9.178 −5.740 1.00 40.25 C ATOM 2649 CB ASN C 97 50.339 10.076 −4.528 1.00 38.65 C ATOM 2650 CG ASN C 97 50.340 9.274 −3.160 1.00 44.04 C ATOM 2651 OD1 ASN C 97 50.540 9.865 −2.086 1.00 43.90 O ATOM 2652 ND2 ASN C 97 50.135 7.962 −3.221 1.00 43.78 N ATOM 2653 C ASN C 97 49.107 8.442 −5.898 1.00 38.81 C ATOM 2654 O ASN C 97 48.018 9.028 −5.895 1.00 39.38 O ATOM 2655 N LYS C 98 49.235 7.141 −5.999 1.00 38.34 N ATOM 2656 CA LYS C 98 48.109 6.210 −6.077 1.00 37.85 C ATOM 2657 CB LYS C 98 48.641 4.910 −6.704 1.00 37.89 C ATOM 2658 CG LYS C 98 49.077 5.156 −8.197 1.00 34.79 C ATOM 2659 CD LYS C 98 49.488 3.865 −8.838 1.00 40.63 C ATOM 2660 CE LYS C 98 49.867 4.054 −10.316 1.00 40.81 C ATOM 2661 NZ LYS C 98 51.073 4.918 −10.448 1.00 38.45 N ATOM 2662 C LYS C 98 47.375 5.892 −4.755 1.00 39.19 C ATOM 2663 O LYS C 98 46.408 5.154 −4.777 1.00 38.96 O ATOM 2664 N GLY C 99 47.858 6.420 −3.636 1.00 38.59 N ATOM 2665 CA GLY C 99 47.449 5.964 −2.296 1.00 40.76 C ATOM 2666 C GLY C 99 47.880 4.530 −2.081 1.00 41.30 C ATOM 2667 O GLY C 99 48.795 4.036 −2.767 1.00 43.80 O ATOM 2668 N ALA C 100 47.248 3.856 −1.143 1.00 40.11 N ATOM 2669 CA ALA C 100 47.560 2.475 −0.883 1.00 39.38 C ATOM 2670 CB ALA C 100 46.860 2.024 0.434 1.00 39.23 C ATOM 2671 C ALA C 100 46.989 1.713 −2.025 1.00 39.51 C ATOM 2672 O ALA C 100 45.893 2.022 −2.468 1.00 39.92 O ATOM 2673 N ILE C 101 47.710 0.705 −2.490 1.00 39.69 N ATOM 2674 CA ILE C 101 47.214 −0.164 −3.542 1.00 39.24 C ATOM 2675 CB ILE C 101 48.382 −0.869 −4.334 1.00 39.71 C ATOM 2676 CG1 ILE C 101 49.331 0.190 −5.017 1.00 39.84 C ATOM 2677 CD1 ILE C 101 48.627 1.159 −5.924 1.00 36.72 C ATOM 2678 CG2 ILE C 101 47.804 −1.860 −5.378 1.00 35.43 C ATOM 2679 C ILE C 101 46.322 −1.192 −2.832 1.00 40.48 C ATOM 2680 O ILE C 101 46.747 −1.835 −1.875 1.00 39.46 O ATOM 2681 N ILE C 102 45.077 −1.290 −3.277 1.00 41.20 N ATOM 2682 CA ILE C 102 44.077 −2.062 −2.594 1.00 42.13 C ATOM 2683 CB ILE C 102 42.722 −1.275 −2.453 1.00 42.58 C ATOM 2684 CG1 ILE C 102 42.912 −0.020 −1.630 1.00 42.57 C ATOM 2685 CD1 ILE C 102 43.084 −0.204 −0.096 1.00 41.89 C ATOM 2686 CG2 ILE C 102 41.542 −2.148 −1.947 1.00 42.41 C ATOM 2687 C ILE C 102 43.887 −3.331 −3.396 1.00 41.41 C ATOM 2688 O ILE C 102 43.698 −4.376 −2.821 1.00 42.57 O ATOM 2689 N GLY C 103 43.942 −3.261 −4.715 1.00 40.57 N ATOM 2690 CA GLY C 103 43.742 −4.479 −5.498 1.00 38.60 C ATOM 2691 C GLY C 103 44.033 −4.305 −6.974 1.00 37.22 C ATOM 2692 O GLY C 103 44.253 −3.238 −7.441 1.00 37.08 O ATOM 2693 N LEU C 104 44.060 −5.393 −7.704 1.00 38.36 N ATOM 2694 CA LEU C 104 44.255 −5.381 −9.148 1.00 39.71 C ATOM 2695 CB LEU C 104 45.653 −5.917 −9.493 1.00 39.02 C ATOM 2696 CG LEU C 104 46.002 −6.069 −10.973 1.00 40.16 C ATOM 2697 CD1 LEU C 104 45.968 −4.664 −11.690 1.00 34.76 C ATOM 2698 CD2 LEU C 104 47.334 −6.727 −11.161 1.00 38.01 C ATOM 2699 C LEU C 104 43.142 −6.283 −9.728 1.00 41.24 C ATOM 2700 O LEU C 104 42.985 −7.408 −9.276 1.00 38.88 O ATOM 2701 N MET C 105 42.368 −5.743 −10.678 1.00 43.67 N ATOM 2702 CA MET C 105 41.297 −6.447 −11.366 1.00 47.58 C ATOM 2703 CB MET C 105 40.101 −5.568 −11.687 1.00 47.39 C ATOM 2704 CG MET C 105 39.496 −4.652 −10.666 1.00 50.10 C ATOM 2705 SD MET C 105 37.752 −4.217 −11.239 1.00 57.87 S ATOM 2706 CE MET C 105 37.532 −4.959 −12.846 1.00 54.27 C ATOM 2707 C MET C 105 41.835 −6.794 −12.704 1.00 47.26 C ATOM 2708 O MET C 105 42.684 −6.094 −13.231 1.00 47.11 O ATOM 2709 N VAL C 106 41.329 −7.879 −13.266 1.00 48.20 N ATOM 2710 CA VAL C 106 41.630 −8.250 −14.630 1.00 49.68 C ATOM 2711 CB VAL C 106 41.031 −9.665 −14.914 1.00 50.52 C ATOM 2712 CG1 VAL C 106 41.298 −10.144 −16.355 1.00 51.88 C ATOM 2713 CG2 VAL C 106 41.664 −10.679 −13.916 1.00 51.57 C ATOM 2714 C VAL C 106 41.214 −7.095 −15.602 1.00 48.70 C ATOM 2715 O VAL C 106 40.269 −6.361 −15.355 1.00 49.46 O ATOM 2716 N GLY C 107 42.012 −6.859 −16.629 1.00 48.36 N ATOM 2717 CA GLY C 107 41.763 −5.713 −17.516 1.00 47.26 C ATOM 2718 C GLY C 107 42.676 −4.536 −17.234 1.00 45.75 C ATOM 2719 O GLY C 107 42.501 −3.459 −17.799 1.00 46.81 O ATOM 2720 N GLY C 108 43.627 −4.736 −16.328 1.00 43.80 N ATOM 2721 CA GLY C 108 44.597 −3.735 −15.974 1.00 42.42 C ATOM 2722 C GLY C 108 44.050 −2.585 −15.171 1.00 41.50 C ATOM 2723 O GLY C 108 44.487 −1.448 −15.371 1.00 43.12 O ATOM 2724 N VAL C 109 43.083 −2.852 −14.304 1.00 39.69 N ATOM 2725 CA VAL C 109 42.387 −1.806 −13.556 1.00 37.50 C ATOM 2726 CB VAL C 109 40.845 −1.962 −13.644 1.00 37.78 C ATOM 2727 CG1 VAL C 109 40.292 −1.715 −15.041 1.00 32.98 C ATOM 2728 CG2 VAL C 109 40.105 −1.033 −12.610 1.00 35.07 C ATOM 2729 C VAL C 109 42.802 −1.942 −12.103 1.00 38.36 C ATOM 2730 O VAL C 109 42.639 −3.027 −11.512 1.00 36.60 O ATOM 2731 N VAL C 110 43.336 −0.870 −11.513 1.00 37.27 N ATOM 2732 CA VAL C 110 43.845 −0.955 −10.160 1.00 37.80 C ATOM 2733 CB VAL C 110 45.245 −0.371 −10.070 1.00 38.39 C ATOM 2734 CG1 VAL C 110 46.115 −1.019 −11.123 1.00 35.91 C ATOM 2735 CG2 VAL C 110 45.851 −0.565 −8.672 1.00 34.68 C ATOM 2736 C VAL C 110 42.897 −0.237 −9.248 1.00 39.02 C ATOM 2737 O VAL C 110 42.247 0.697 −9.695 1.00 38.55 O ATOM 2738 N ILE C 111 42.743 −0.718 −8.010 1.00 39.64 N ATOM 2739 CA ILE C 111 41.985 −0.007 −6.976 1.00 40.38 C ATOM 2740 CB ILE C 111 41.039 −0.966 −6.233 1.00 40.84 C ATOM 2741 CG1 ILE C 111 40.202 −1.806 −7.257 1.00 43.74 C ATOM 2742 CD1 ILE C 111 39.645 −3.116 −6.586 1.00 44.34 C ATOM 2743 CG2 ILE C 111 40.111 −0.240 −5.264 1.00 40.12 C ATOM 2744 C ILE C 111 42.995 0.553 −6.005 1.00 40.90 C ATOM 2745 O ILE C 111 43.911 −0.155 −5.522 1.00 40.15 O ATOM 2746 N GLY C 112 42.870 1.839 −5.722 1.00 41.79 N ATOM 2747 CA GLY C 112 43.727 2.465 −4.695 1.00 41.67 C ATOM 2748 C GLY C 112 42.804 3.024 −3.631 1.00 42.53 C ATOM 2749 O GLY C 112 41.599 3.097 −3.837 1.00 42.69 O ATOM 2750 N GLY C 113 43.352 3.378 −2.479 1.00 42.32 N ATOM 2751 CA GLY C 113 42.544 3.983 −1.444 1.00 42.68 C ATOM 2752 C GLY C 113 43.431 4.872 −0.602 1.00 43.14 C ATOM 2753 O GLY C 113 44.645 4.595 −0.482 1.00 42.77 O ATOM 2754 N GLU C 114 42.829 5.961 −0.105 1.00 43.84 N ATOM 2755 CA GLU C 114 43.389 6.874 0.895 1.00 45.57 C ATOM 2756 CB GLU C 114 43.530 8.314 0.328 1.00 46.12 C ATOM 2757 CG GLU C 114 44.677 8.540 −0.659 1.00 48.41 C ATOM 2758 CD GLU C 114 46.012 8.648 0.104 1.00 53.32 C ATOM 2759 OE1 GLU C 114 45.961 8.894 1.318 1.00 54.08 O ATOM 2760 OE2 GLU C 114 47.105 8.460 −0.484 1.00 53.74 O ATOM 2761 C GLU C 114 42.434 6.922 2.110 1.00 45.53 C ATOM 2762 O GLU C 114 41.258 7.185 1.933 1.00 44.18 O ATOM 2763 N LYS C 115 42.973 6.750 3.330 1.00 45.32 N ATOM 2764 CA LYS C 115 42.202 6.844 4.591 1.00 44.84 C ATOM 2765 CB LYS C 115 42.676 5.771 5.567 1.00 46.12 C ATOM 2766 CG LYS C 115 42.435 4.362 5.125 1.00 51.00 C ATOM 2767 CD LYS C 115 42.795 3.392 6.277 1.00 58.28 C ATOM 2768 CE LYS C 115 41.567 2.885 7.055 1.00 57.90 C ATOM 2769 NZ LYS C 115 41.949 1.742 8.016 1.00 54.76 N ATOM 2770 C LYS C 115 42.365 8.197 5.290 1.00 44.22 C ATOM 2771 O LYS C 115 43.431 8.823 5.252 1.00 43.62 O ATOM 2772 N GLY C 116 41.305 8.645 5.954 1.00 43.05 N ATOM 2773 CA GLY C 116 41.356 9.864 6.689 1.00 42.05 C ATOM 2774 C GLY C 116 42.174 9.631 7.930 1.00 42.35 C ATOM 2775 O GLY C 116 42.452 8.484 8.287 1.00 42.05 O ATOM 2776 N ALA C 117 42.571 10.708 8.596 1.00 42.37 N ATOM 2777 CA ALA C 117 43.399 10.550 9.757 1.00 43.05 C ATOM 2778 CB ALA C 117 44.260 11.829 10.014 1.00 42.67 C ATOM 2779 C ALA C 117 42.634 10.084 11.023 1.00 43.56 C ATOM 2780 O ALA C 117 43.246 9.826 12.055 1.00 43.65 O ATOM 2781 N GLY C 118 41.314 9.951 10.965 1.00 43.66 N ATOM 2782 CA GLY C 118 40.611 9.472 12.152 1.00 42.79 C ATOM 2783 C GLY C 118 39.896 10.562 12.934 1.00 41.73 C ATOM 2784 O GLY C 118 40.354 11.701 12.976 1.00 40.92 O ATOM 2785 N THR C 119 38.743 10.194 13.496 1.00 39.98 N ATOM 2786 CA THR C 119 37.946 11.020 14.384 1.00 38.58 C ATOM 2787 CB THR C 119 36.488 11.253 13.783 1.00 39.57 C ATOM 2788 OG1 THR C 119 36.588 12.076 12.602 1.00 38.54 O ATOM 2789 CG2 THR C 119 35.520 11.976 14.801 1.00 36.85 C ATOM 2790 C THR C 119 37.848 10.245 15.679 1.00 38.20 C ATOM 2791 O THR C 119 37.235 9.181 15.707 1.00 38.00 O ATOM 2792 N ALA C 120 38.444 10.762 16.760 1.00 39.02 N ATOM 2793 CA ALA C 120 38.267 10.190 18.104 1.00 38.01 C ATOM 2794 CB ALA C 120 39.460 10.554 19.000 1.00 37.67 C ATOM 2795 C ALA C 120 36.956 10.710 18.698 1.00 38.14 C ATOM 2796 O ALA C 120 36.900 11.849 19.022 1.00 38.99 O ATOM 2797 N LEU C 121 35.904 9.888 18.786 1.00 37.88 N ATOM 2798 CA LEU C 121 34.606 10.267 19.338 1.00 37.54 C ATOM 2799 CB LEU C 121 33.405 9.771 18.456 1.00 37.32 C ATOM 2800 CG LEU C 121 32.005 9.892 19.096 1.00 36.95 C ATOM 2801 CD1 LEU C 121 31.645 11.412 19.345 1.00 30.48 C ATOM 2802 CD2 LEU C 121 30.953 9.178 18.323 1.00 36.88 C ATOM 2803 C LEU C 121 34.449 9.684 20.736 1.00 39.77 C ATOM 2804 O LEU C 121 34.550 8.474 20.921 1.00 39.94 O ATOM 2805 N THR C 122 34.231 10.558 21.715 1.00 39.58 N ATOM 2806 CA THR C 122 33.743 10.128 23.012 1.00 42.41 C ATOM 2807 CB THR C 122 34.744 10.283 24.221 1.00 42.49 C ATOM 2808 OG1 THR C 122 34.066 10.807 25.351 1.00 47.39 O ATOM 2809 CG2 THR C 122 35.975 11.103 23.923 1.00 44.50 C ATOM 2810 C THR C 122 32.368 10.695 23.269 1.00 41.60 C ATOM 2811 O THR C 122 32.115 11.879 22.992 1.00 40.70 O ATOM 2812 N VAL C 123 31.465 9.800 23.664 1.00 41.20 N ATOM 2813 CA VAL C 123 30.065 10.141 23.928 1.00 41.97 C ATOM 2814 CB VAL C 123 29.040 9.174 23.218 1.00 41.64 C ATOM 2815 CG1 VAL C 123 27.572 9.521 23.597 1.00 38.86 C ATOM 2816 CG2 VAL C 123 29.222 9.177 21.701 1.00 36.97 C ATOM 2817 C VAL C 123 29.901 10.060 25.442 1.00 43.60 C ATOM 2818 O VAL C 123 30.189 9.036 26.029 1.00 43.27 O ATOM 2819 N LYS C 124 29.459 11.137 26.070 1.00 46.27 N ATOM 2820 CA LYS C 124 29.335 11.162 27.519 1.00 50.07 C ATOM 2821 CB LYS C 124 29.566 12.574 28.019 1.00 51.04 C ATOM 2822 CG LYS C 124 30.992 13.088 27.721 1.00 55.46 C ATOM 2823 CD LYS C 124 31.184 14.509 28.264 1.00 62.63 C ATOM 2824 CE LYS C 124 30.287 15.512 27.491 1.00 64.83 C ATOM 2825 NZ LYS C 124 30.202 16.850 28.169 1.00 67.51 N ATOM 2826 C LYS C 124 27.960 10.729 27.900 1.00 51.41 C ATOM 2827 O LYS C 124 27.006 11.094 27.223 1.00 53.12 O ATOM 2828 N ALA C 125 27.857 9.965 28.982 1.00 53.39 N ATOM 2829 CA ALA C 125 26.584 9.427 29.504 1.00 55.35 C ATOM 2830 CB ALA C 125 26.828 8.627 30.778 1.00 54.28 C ATOM 2831 C ALA C 125 25.485 10.460 29.739 1.00 57.36 C ATOM 2832 O ALA C 125 25.745 11.656 29.989 1.00 56.29 O ATOM 2833 N ALA C 126 24.240 9.987 29.654 1.00 60.08 N ATOM 2834 CA ALA C 126 23.084 10.865 29.877 1.00 62.33 C ATOM 2835 CB ALA C 126 21.766 10.076 29.780 1.00 62.64 C ATOM 2836 C ALA C 126 23.246 11.540 31.244 1.00 63.68 C ATOM 2837 O ALA C 126 23.436 10.871 32.272 1.00 64.15 O ATOM 2838 OXT ALA C 126 23.253 12.783 31.350 1.00 65.04 O ATOM 2839 N ALA D 1 46.173 −30.720 −12.181 1.00 52.41 N ATOM 2840 CA ALA D 1 47.352 −29.997 −11.635 1.00 52.38 C ATOM 2841 CB ALA D 1 47.073 −28.463 −11.586 1.00 52.73 C ATOM 2842 C ALA D 1 47.756 −30.484 −10.247 1.00 52.06 C ATOM 2843 O ALA D 1 47.324 −29.889 −9.245 1.00 52.92 O ATOM 2844 N TRP D 2 48.618 −31.503 −10.174 1.00 50.77 N ATOM 2845 CA TRP D 2 49.207 −31.901 −8.886 1.00 49.15 C ATOM 2846 CB TRP D 2 48.379 −33.027 −8.243 1.00 49.04 C ATOM 2847 CG TRP D 2 48.455 −34.342 −8.948 1.00 48.39 C ATOM 2848 CD1 TRP D 2 47.909 −34.665 −10.162 1.00 48.80 C ATOM 2849 NE1 TRP D 2 48.181 −35.993 −10.473 1.00 47.88 N ATOM 2850 CE2 TRP D 2 48.915 −36.540 −9.456 1.00 48.78 C ATOM 2851 CD2 TRP D 2 49.105 −35.532 −8.474 1.00 48.50 C ATOM 2852 CE3 TRP D 2 49.816 −35.851 −7.312 1.00 49.44 C ATOM 2853 CZ3 TRP D 2 50.318 −37.152 −7.169 1.00 48.14 C ATOM 2854 CH2 TRP D 2 50.130 −38.111 −8.167 1.00 48.46 C ATOM 2855 CZ2 TRP D 2 49.430 −37.833 −9.311 1.00 48.68 C ATOM 2856 C TRP D 2 50.692 −32.283 −8.969 1.00 48.37 C ATOM 2857 O TRP D 2 51.129 −32.808 −9.982 1.00 47.97 O ATOM 2858 N VAL D 3 51.447 −32.014 −7.892 1.00 47.21 N ATOM 2859 CA VAL D 3 52.880 −32.359 −7.783 1.00 46.09 C ATOM 2860 CB VAL D 3 53.713 −31.248 −7.051 1.00 45.63 C ATOM 2861 CG1 VAL D 3 55.086 −31.739 −6.681 1.00 45.70 C ATOM 2862 CG2 VAL D 3 53.857 −30.036 −7.931 1.00 45.94 C ATOM 2863 C VAL D 3 53.042 −33.724 −7.090 1.00 45.51 C ATOM 2864 O VAL D 3 52.541 −33.953 −5.995 1.00 45.34 O ATOM 2865 N ASP D 4 53.726 −34.629 −7.766 1.00 44.30 N ATOM 2866 CA ASP D 4 53.861 −36.002 −7.344 1.00 43.85 C ATOM 2867 CB ASP D 4 53.638 −36.897 −8.574 1.00 43.56 C ATOM 2868 CG ASP D 4 53.731 −38.385 −8.283 1.00 46.38 C ATOM 2869 OD1 ASP D 4 53.456 −39.152 −9.224 1.00 48.84 O ATOM 2870 OD2 ASP D 4 54.085 −38.824 −7.165 1.00 49.73 O ATOM 2871 C ASP D 4 55.282 −36.096 −6.773 1.00 42.85 C ATOM 2872 O ASP D 4 56.260 −36.173 −7.527 1.00 43.36 O ATOM 2873 N GLN D 5 55.399 −36.044 −5.450 1.00 40.53 N ATOM 2874 CA GLN D 5 56.695 −36.068 −4.816 1.00 39.40 C ATOM 2875 CB GLN D 5 56.769 −34.988 −3.723 1.00 38.84 C ATOM 2876 CG GLN D 5 58.080 −34.973 −2.919 1.00 37.60 C ATOM 2877 CD GLN D 5 58.067 −33.903 −1.836 1.00 40.37 C ATOM 2878 OE1 GLN D 5 57.169 −33.053 −1.805 1.00 39.68 O ATOM 2879 NE2 GLN D 5 59.067 −33.928 −0.944 1.00 37.57 N ATOM 2880 C GLN D 5 56.978 −37.445 −4.208 1.00 39.58 C ATOM 2881 O GLN D 5 56.165 −37.959 −3.443 1.00 39.26 O ATOM 2882 N THR D 6 58.153 −37.997 −4.531 1.00 39.50 N ATOM 2883 CA THR D 6 58.650 −39.281 −4.032 1.00 39.81 C ATOM 2884 CB THR D 6 58.637 −40.379 −5.152 1.00 39.82 C ATOM 2885 OG1 THR D 6 59.280 −39.861 −6.318 1.00 41.35 O ATOM 2886 CG2 THR D 6 57.202 −40.812 −5.536 1.00 41.10 C ATOM 2887 C THR D 6 60.103 −39.129 −3.536 1.00 39.11 C ATOM 2888 O THR D 6 60.846 −38.306 −4.047 1.00 38.91 O ATOM 2889 N PRO D 7 60.509 −39.925 −2.532 1.00 38.82 N ATOM 2890 CA PRO D 7 59.674 −40.854 −1.771 1.00 38.84 C ATOM 2891 CB PRO D 7 60.708 −41.859 −1.250 1.00 39.29 C ATOM 2892 CG PRO D 7 61.982 −40.990 −1.047 1.00 38.10 C ATOM 2893 CD PRO D 7 61.918 −39.932 −2.080 1.00 38.51 C ATOM 2894 C PRO D 7 58.938 −40.128 −0.616 1.00 38.96 C ATOM 2895 O PRO D 7 59.364 −39.093 −0.218 1.00 38.31 O ATOM 2896 N ARG D 8 57.835 −40.664 −0.098 1.00 40.27 N ATOM 2897 CA ARG D 8 57.128 −40.039 1.046 1.00 40.80 C ATOM 2898 CB ARG D 8 55.743 −40.686 1.236 1.00 40.70 C ATOM 2899 CG ARG D 8 54.775 −40.011 2.223 1.00 45.33 C ATOM 2900 CD ARG D 8 54.283 −38.614 1.746 1.00 52.07 C ATOM 2901 NE ARG D 8 54.080 −38.557 0.289 1.00 54.98 N ATOM 2902 CZ ARG D 8 52.900 −38.616 −0.330 1.00 57.24 C ATOM 2903 NH1 ARG D 8 51.758 −38.714 0.359 1.00 56.56 N ATOM 2904 NH2 ARG D 8 52.862 −38.549 −1.658 1.00 58.04 N ATOM 2905 C ARG D 8 57.977 −40.100 2.331 1.00 40.53 C ATOM 2906 O ARG D 8 57.929 −39.207 3.158 1.00 40.81 O ATOM 2907 N THR D 9 58.770 −41.153 2.475 1.00 40.47 N ATOM 2908 CA THR D 9 59.629 −41.350 3.634 1.00 40.91 C ATOM 2909 CB THR D 9 58.994 −42.340 4.695 1.00 41.45 C ATOM 2910 OG1 THR D 9 58.726 −43.600 4.084 1.00 41.04 O ATOM 2911 CG2 THR D 9 57.639 −41.805 5.351 1.00 41.38 C ATOM 2912 C THR D 9 60.999 −41.914 3.169 1.00 41.67 C ATOM 2913 O THR D 9 61.083 −42.696 2.225 1.00 40.23 O ATOM 2914 N ALA D 10 62.064 −41.522 3.868 1.00 42.06 N ATOM 2915 CA ALA D 10 63.392 −42.065 3.635 1.00 41.77 C ATOM 2916 CB ALA D 10 64.160 −41.142 2.735 1.00 42.21 C ATOM 2917 C ALA D 10 64.086 −42.181 4.998 1.00 42.56 C ATOM 2918 O ALA D 10 63.811 −41.387 5.903 1.00 40.53 O ATOM 2919 N THR D 11 64.914 −43.211 5.161 1.00 43.58 N ATOM 2920 CA THR D 11 65.800 −43.354 6.320 1.00 45.06 C ATOM 2921 CB THR D 11 65.427 −44.561 7.235 1.00 45.98 C ATOM 2922 OG1 THR D 11 64.100 −44.386 7.754 1.00 48.35 O ATOM 2923 CG2 THR D 11 66.423 −44.712 8.442 1.00 45.10 C ATOM 2924 C THR D 11 67.177 −43.562 5.723 1.00 46.01 C ATOM 2925 O THR D 11 67.379 −44.392 4.825 1.00 46.79 O ATOM 2926 N LYS D 12 68.118 −42.766 6.193 1.00 46.59 N ATOM 2927 CA LYS D 12 69.488 −42.806 5.725 1.00 46.11 C ATOM 2928 CB LYS D 12 69.766 −41.586 4.863 1.00 45.49 C ATOM 2929 CG LYS D 12 68.877 −41.544 3.598 1.00 44.78 C ATOM 2930 CD LYS D 12 69.231 −42.666 2.588 1.00 40.67 C ATOM 2931 CE LYS D 12 68.264 −42.658 1.445 1.00 42.32 C ATOM 2932 NZ LYS D 12 68.712 −43.565 0.374 1.00 41.82 N ATOM 2933 C LYS D 12 70.441 −42.847 6.903 1.00 47.39 C ATOM 2934 O LYS D 12 70.080 −42.564 8.065 1.00 46.27 O ATOM 2935 N GLU D 13 71.669 −43.213 6.583 1.00 48.57 N ATOM 2936 CA GLU D 13 72.742 −43.190 7.538 1.00 49.48 C ATOM 2937 CB GLU D 13 73.578 −44.461 7.335 1.00 50.69 C ATOM 2938 CG GLU D 13 73.899 −45.243 8.610 1.00 53.61 C ATOM 2939 CD GLU D 13 75.339 −45.752 8.601 1.00 59.15 C ATOM 2940 OE1 GLU D 13 75.609 −46.771 9.288 1.00 59.36 O ATOM 2941 OE2 GLU D 13 76.200 −45.139 7.892 1.00 59.86 O ATOM 2942 C GLU D 13 73.534 −41.911 7.193 1.00 48.81 C ATOM 2943 O GLU D 13 73.480 −41.453 6.043 1.00 48.11 O ATOM 2944 N THR D 14 74.259 −41.324 8.155 1.00 48.09 N ATOM 2945 CA THR D 14 75.143 −40.192 7.810 1.00 47.65 C ATOM 2946 CB THR D 14 75.925 −39.621 9.031 1.00 47.59 C ATOM 2947 OG1 THR D 14 76.628 −40.678 9.687 1.00 48.03 O ATOM 2948 CG2 THR D 14 74.987 −38.998 10.048 1.00 47.29 C ATOM 2949 C THR D 14 76.117 −40.593 6.681 1.00 47.56 C ATOM 2950 O THR D 14 76.583 −41.748 6.620 1.00 47.03 O ATOM 2951 N GLY D 15 76.414 −39.648 5.793 1.00 46.77 N ATOM 2952 CA GLY D 15 77.304 −39.915 4.667 1.00 46.69 C ATOM 2953 C GLY D 15 76.607 −40.296 3.367 1.00 46.34 C ATOM 2954 O GLY D 15 77.083 −39.969 2.293 1.00 46.24 O ATOM 2955 N GLU D 16 75.484 −40.998 3.474 1.00 46.52 N ATOM 2956 CA GLU D 16 74.670 −41.389 2.327 1.00 46.87 C ATOM 2957 CB GLU D 16 73.574 −42.384 2.757 1.00 46.63 C ATOM 2958 CG GLU D 16 74.023 −43.586 3.578 1.00 46.69 C ATOM 2959 CD GLU D 16 72.979 −44.733 3.575 1.00 48.35 C ATOM 2960 OE1 GLU D 16 73.193 −45.693 2.807 1.00 53.70 O ATOM 2961 OE2 GLU D 16 71.954 −44.705 4.299 1.00 48.55 O ATOM 2962 C GLU D 16 74.003 −40.187 1.632 1.00 46.94 C ATOM 2963 O GLU D 16 74.209 −39.019 1.977 1.00 46.67 O ATOM 2964 N SER D 17 73.174 −40.471 0.637 1.00 47.38 N ATOM 2965 CA SER D 17 72.518 −39.376 −0.056 1.00 47.46 C ATOM 2966 CB SER D 17 73.184 −39.131 −1.410 1.00 48.28 C ATOM 2967 OG SER D 17 72.749 −40.047 −2.416 1.00 52.49 O ATOM 2968 C SER D 17 71.029 −39.642 −0.196 1.00 46.61 C ATOM 2969 O SER D 17 70.588 −40.785 0.001 1.00 46.62 O ATOM 2970 N LEU D 18 70.263 −38.583 −0.477 1.00 44.97 N ATOM 2971 CA LEU D 18 68.829 −38.674 −0.742 1.00 43.88 C ATOM 2972 CB LEU D 18 68.010 −37.924 0.319 1.00 44.17 C ATOM 2973 CG LEU D 18 66.612 −38.336 0.802 1.00 44.22 C ATOM 2974 CD1 LEU D 18 65.730 −37.114 0.965 1.00 44.33 C ATOM 2975 CD2 LEU D 18 65.950 −39.375 −0.033 1.00 43.22 C ATOM 2976 C LEU D 18 68.614 −37.943 −2.049 1.00 43.24 C ATOM 2977 O LEU D 18 69.159 −36.865 −2.231 1.00 42.98 O ATOM 2978 N THR D 19 67.817 −38.528 −2.936 1.00 42.05 N ATOM 2979 CA THR D 19 67.259 −37.821 −4.062 1.00 41.13 C ATOM 2980 CB THR D 19 67.673 −38.509 −5.373 1.00 41.27 C ATOM 2981 OG1 THR D 19 68.982 −39.032 −5.185 1.00 42.63 O ATOM 2982 CG2 THR D 19 67.703 −37.531 −6.542 1.00 39.59 C ATOM 2983 C THR D 19 65.731 −37.751 −3.892 1.00 40.45 C ATOM 2984 O THR D 19 65.055 −38.763 −3.753 1.00 40.58 O ATOM 2985 N ILE D 20 65.207 −36.542 −3.859 1.00 39.89 N ATOM 2986 CA ILE D 20 63.766 −36.329 −3.894 1.00 40.16 C ATOM 2987 CB ILE D 20 63.326 −35.181 −2.940 1.00 40.54 C ATOM 2988 CG1 ILE D 20 63.757 −35.493 −1.505 1.00 41.28 C ATOM 2989 CD1 ILE D 20 63.883 −34.280 −0.649 1.00 41.55 C ATOM 2990 CG2 ILE D 20 61.799 −34.926 −3.043 1.00 39.20 C ATOM 2991 C ILE D 20 63.383 −35.979 −5.323 1.00 39.22 C ATOM 2992 O ILE D 20 64.012 −35.141 −5.904 1.00 38.55 O ATOM 2993 N ASN D 21 62.358 −36.632 −5.859 1.00 39.57 N ATOM 2994 CA ASN D 21 61.852 −36.370 −7.213 1.00 41.08 C ATOM 2995 CB ASN D 21 61.773 −37.676 −7.967 1.00 41.24 C ATOM 2996 CG ASN D 21 63.008 −37.956 −8.759 1.00 43.85 C ATOM 2997 OD1 ASN D 21 63.215 −37.323 −9.793 1.00 48.63 O ATOM 2998 ND2 ASN D 21 63.814 −38.942 −8.325 1.00 43.95 N ATOM 2999 C ASN D 21 60.453 −35.779 −7.184 1.00 41.77 C ATOM 3000 O ASN D 21 59.636 −36.200 −6.375 1.00 41.70 O ATOM 3001 N CYS D 22 60.180 −34.794 −8.039 1.00 42.41 N ATOM 3002 CA CYS D 22 58.840 −34.207 −8.137 1.00 43.48 C ATOM 3003 CB CYS D 22 58.774 −32.833 −7.476 1.00 42.75 C ATOM 3004 SG CYS D 22 59.105 −32.836 −5.677 1.00 49.46 S ATOM 3005 C CYS D 22 58.428 −34.062 −9.580 1.00 43.16 C ATOM 3006 O CYS D 22 59.168 −33.495 −10.359 1.00 43.59 O ATOM 3007 N VAL D 23 57.228 −34.523 −9.918 1.00 43.81 N ATOM 3008 CA VAL D 23 56.647 −34.300 −11.241 1.00 44.50 C ATOM 3009 CB VAL D 23 56.382 −35.665 −11.979 1.00 44.28 C ATOM 3010 CG1 VAL D 23 55.931 −35.444 −13.468 1.00 44.41 C ATOM 3011 CG2 VAL D 23 57.614 −36.588 −11.902 1.00 42.56 C ATOM 3012 C VAL D 23 55.358 −33.477 −11.126 1.00 45.73 C ATOM 3013 O VAL D 23 54.510 −33.746 −10.265 1.00 45.32 O ATOM 3014 N LEU D 24 55.224 −32.460 −11.986 1.00 47.64 N ATOM 3015 CA LEU D 24 53.951 −31.724 −12.179 1.00 48.97 C ATOM 3016 CB LEU D 24 54.214 −30.344 −12.795 1.00 48.56 C ATOM 3017 CG LEU D 24 53.466 −29.079 −12.328 1.00 49.30 C ATOM 3018 CD1 LEU D 24 53.669 −27.924 −13.368 1.00 46.03 C ATOM 3019 CD2 LEU D 24 51.974 −29.319 −11.999 1.00 48.04 C ATOM 3020 C LEU D 24 52.983 −32.521 −13.083 1.00 49.95 C ATOM 3021 O LEU D 24 53.134 −32.529 −14.313 1.00 50.57 O ATOM 3022 N ARG D 25 52.001 −33.195 −12.471 1.00 51.10 N ATOM 3023 CA ARG D 25 51.019 −34.050 −13.192 1.00 51.64 C ATOM 3024 CB ARG D 25 50.696 −35.313 −12.386 1.00 51.32 C ATOM 3025 CG ARG D 25 51.863 −36.063 −11.871 1.00 49.97 C ATOM 3026 CD ARG D 25 52.204 −37.166 −12.794 1.00 47.93 C ATOM 3027 NE ARG D 25 53.274 −37.967 −12.225 1.00 47.52 N ATOM 3028 CZ ARG D 25 53.981 −38.861 −12.909 1.00 47.68 C ATOM 3029 NH1 ARG D 25 53.741 −39.083 −14.202 1.00 46.46 N ATOM 3030 NH2 ARG D 25 54.941 −39.536 −12.298 1.00 48.61 N ATOM 3031 C ARG D 25 49.699 −33.318 −13.473 1.00 52.55 C ATOM 3032 O ARG D 25 49.412 −32.286 −12.847 1.00 52.60 O ATOM 3033 N ASP D 26 48.891 −33.884 −14.386 1.00 53.55 N ATOM 3034 CA ASP D 26 47.619 −33.276 −14.857 1.00 54.33 C ATOM 3035 CB ASP D 26 46.477 −33.475 −13.843 1.00 54.58 C ATOM 3036 CG ASP D 26 45.374 −34.384 −14.368 1.00 55.93 C ATOM 3037 OD1 ASP D 26 44.789 −34.090 −15.443 1.00 57.14 O ATOM 3038 OD2 ASP D 26 45.089 −35.398 −13.694 1.00 57.19 O ATOM 3039 C ASP D 26 47.694 −31.801 −15.233 1.00 54.37 C ATOM 3040 O ASP D 26 46.708 −31.085 −15.092 1.00 54.79 O ATOM 3041 N ALA D 27 48.845 −31.346 −15.719 1.00 54.73 N ATOM 3042 CA ALA D 27 49.050 −29.918 −15.985 1.00 54.79 C ATOM 3043 CB ALA D 27 50.415 −29.475 −15.472 1.00 54.57 C ATOM 3044 C ALA D 27 48.897 −29.583 −17.469 1.00 54.93 C ATOM 3045 O ALA D 27 49.543 −30.202 −18.321 1.00 55.09 O ATOM 3046 N SER D 28 48.038 −28.617 −17.781 1.00 54.75 N ATOM 3047 CA SER D 28 47.935 −28.133 −19.152 1.00 54.93 C ATOM 3048 CB SER D 28 46.488 −27.753 −19.510 1.00 55.22 C ATOM 3049 OG SER D 28 46.074 −26.557 −18.862 1.00 55.13 O ATOM 3050 C SER D 28 48.892 −26.952 −19.338 1.00 54.84 C ATOM 3051 O SER D 28 49.138 −26.492 −20.463 1.00 54.36 O ATOM 3052 N PHE D 29 49.413 −26.472 −18.209 1.00 54.77 N ATOM 3053 CA PHE D 29 50.460 −25.448 −18.167 1.00 54.65 C ATOM 3054 CB PHE D 29 50.152 −24.392 −17.096 1.00 55.22 C ATOM 3055 CG PHE D 29 49.499 −24.951 −15.847 1.00 56.31 C ATOM 3056 CD1 PHE D 29 50.206 −25.806 −14.988 1.00 56.26 C ATOM 3057 CE1 PHE D 29 49.596 −26.332 −13.834 1.00 57.52 C ATOM 3058 CZ PHE D 29 48.269 −25.993 −13.528 1.00 57.03 C ATOM 3059 CE2 PHE D 29 47.554 −25.124 −14.385 1.00 58.39 C ATOM 3060 CD2 PHE D 29 48.174 −24.614 −15.534 1.00 56.93 C ATOM 3061 C PHE D 29 51.867 −26.058 −17.966 1.00 54.11 C ATOM 3062 O PHE D 29 52.019 −27.269 −17.723 1.00 53.85 O ATOM 3063 N GLU D 30 52.884 −25.210 −18.091 1.00 53.36 N ATOM 3064 CA GLU D 30 54.270 −25.660 −18.088 1.00 52.94 C ATOM 3065 CB GLU D 30 55.046 −25.061 −19.275 1.00 53.22 C ATOM 3066 CG GLU D 30 54.424 −25.259 −20.663 1.00 54.41 C ATOM 3067 CD GLU D 30 54.848 −26.554 −21.333 1.00 56.12 C ATOM 3068 OE1 GLU D 30 55.997 −27.002 −21.121 1.00 57.05 O ATOM 3069 OE2 GLU D 30 54.028 −27.124 −22.079 1.00 56.87 O ATOM 3070 C GLU D 30 54.947 −25.262 −16.778 1.00 51.85 C ATOM 3071 O GLU D 30 54.501 −24.352 −16.081 1.00 51.46 O ATOM 3072 N LEU D 31 56.045 −25.942 −16.474 1.00 51.22 N ATOM 3073 CA LEU D 31 56.825 −25.688 −15.275 1.00 49.86 C ATOM 3074 CB LEU D 31 57.710 −26.901 −14.991 1.00 49.53 C ATOM 3075 CG LEU D 31 58.340 −26.964 −13.595 1.00 48.63 C ATOM 3076 CD1 LEU D 31 57.315 −26.642 −12.490 1.00 43.48 C ATOM 3077 CD2 LEU D 31 58.957 −28.337 −13.398 1.00 46.35 C ATOM 3078 C LEU D 31 57.695 −24.468 −15.489 1.00 49.34 C ATOM 3079 O LEU D 31 58.652 −24.527 −16.250 1.00 49.11 O ATOM 3080 N LYS D 32 57.362 −23.366 −14.838 1.00 49.24 N ATOM 3081 CA LYS D 32 58.155 −22.156 −14.986 1.00 49.60 C ATOM 3082 CB LYS D 32 57.325 −20.901 −14.692 1.00 49.77 C ATOM 3083 CG LYS D 32 56.343 −20.516 −15.862 1.00 51.34 C ATOM 3084 CD LYS D 32 56.909 −20.827 −17.265 1.00 50.23 C ATOM 3085 CE LYS D 32 55.918 −20.497 −18.363 1.00 51.66 C ATOM 3086 NZ LYS D 32 55.711 −21.653 −19.277 1.00 51.95 N ATOM 3087 C LYS D 32 59.398 −22.205 −14.111 1.00 50.13 C ATOM 3088 O LYS D 32 60.530 −22.068 −14.608 1.00 50.59 O ATOM 3089 N ASP D 33 59.174 −22.422 −12.820 1.00 48.97 N ATOM 3090 CA ASP D 33 60.207 −22.327 −11.799 1.00 49.30 C ATOM 3091 CB ASP D 33 60.268 −20.869 −11.293 1.00 49.60 C ATOM 3092 CG ASP D 33 61.514 −20.592 −10.464 1.00 54.11 C ATOM 3093 OD1 ASP D 33 62.644 −21.000 −10.869 1.00 55.49 O ATOM 3094 OD2 ASP D 33 61.356 −19.998 −9.367 1.00 59.32 O ATOM 3095 C ASP D 33 59.965 −23.362 −10.629 1.00 47.92 C ATOM 3096 O ASP D 33 58.887 −23.942 −10.506 1.00 47.18 O ATOM 3097 N THR D 34 60.964 −23.576 −9.782 1.00 47.12 N ATOM 3098 CA THR D 34 60.882 −24.571 −8.714 1.00 45.90 C ATOM 3099 CB THR D 34 61.701 −25.848 −9.054 1.00 46.44 C ATOM 3100 OG1 THR D 34 63.095 −25.523 −9.217 1.00 43.45 O ATOM 3101 CG2 THR D 34 61.172 −26.526 −10.312 1.00 46.59 C ATOM 3102 C THR D 34 61.449 −24.004 −7.427 1.00 46.20 C ATOM 3103 O THR D 34 62.340 −23.122 −7.464 1.00 46.30 O ATOM 3104 N GLY D 35 60.944 −24.509 −6.290 1.00 45.15 N ATOM 3105 CA GLY D 35 61.530 −24.211 −4.995 1.00 44.20 C ATOM 3106 C GLY D 35 61.560 −25.447 −4.130 1.00 44.10 C ATOM 3107 O GLY D 35 60.734 −26.358 −4.309 1.00 43.01 O ATOM 3108 N TRP D 36 62.497 −25.440 −3.172 1.00 43.91 N ATOM 3109 CA TRP D 36 62.680 −26.524 −2.222 1.00 43.17 C ATOM 3110 CB TRP D 36 63.989 −27.274 −2.505 1.00 42.16 C ATOM 3111 CG TRP D 36 63.897 −28.084 −3.748 1.00 42.33 C ATOM 3112 CD1 TRP D 36 64.287 −27.709 −4.990 1.00 41.86 C ATOM 3113 NE1 TRP D 36 64.020 −28.710 −5.901 1.00 41.80 N ATOM 3114 CE2 TRP D 36 63.440 −29.761 −5.246 1.00 39.28 C ATOM 3115 CD2 TRP D 36 63.339 −29.404 −3.881 1.00 41.23 C ATOM 3116 CE3 TRP D 36 62.771 −30.315 −2.975 1.00 40.97 C ATOM 3117 CZ3 TRP D 36 62.320 −31.538 −3.462 1.00 41.67 C ATOM 3118 CH2 TRP D 36 62.442 −31.859 −4.835 1.00 42.09 C ATOM 3119 CZ2 TRP D 36 63.008 −30.988 −5.737 1.00 39.64 C ATOM 3120 C TRP D 36 62.666 −25.949 −0.848 1.00 43.26 C ATOM 3121 O TRP D 36 63.284 −24.931 −0.618 1.00 42.62 O ATOM 3122 N TYR D 37 61.921 −26.603 0.042 1.00 43.77 N ATOM 3123 CA TYR D 37 61.774 −26.215 1.445 1.00 44.44 C ATOM 3124 CB TYR D 37 60.384 −25.667 1.724 1.00 45.80 C ATOM 3125 CG TYR D 37 59.912 −24.825 0.615 1.00 50.24 C ATOM 3126 CD1 TYR D 37 60.243 −23.457 0.557 1.00 52.74 C ATOM 3127 CE1 TYR D 37 59.827 −22.661 −0.510 1.00 53.61 C ATOM 3128 CZ TYR D 37 59.078 −23.238 −1.534 1.00 53.15 C ATOM 3129 OH TYR D 37 58.677 −22.491 −2.597 1.00 53.11 O ATOM 3130 CE2 TYR D 37 58.744 −24.592 −1.499 1.00 53.55 C ATOM 3131 CD2 TYR D 37 59.167 −25.382 −0.419 1.00 51.12 C ATOM 3132 C TYR D 37 61.987 −27.398 2.367 1.00 43.19 C ATOM 3133 O TYR D 37 61.769 −28.539 1.964 1.00 41.62 O ATOM 3134 N ARG D 38 62.305 −27.064 3.620 1.00 42.47 N ATOM 3135 CA ARG D 38 62.552 −28.009 4.705 1.00 43.75 C ATOM 3136 CB ARG D 38 64.045 −28.379 4.717 1.00 43.86 C ATOM 3137 CG ARG D 38 64.576 −28.648 6.062 1.00 48.19 C ATOM 3138 CD ARG D 38 65.373 −29.910 6.170 1.00 53.19 C ATOM 3139 NE ARG D 38 66.808 −29.728 5.932 1.00 58.72 N ATOM 3140 CZ ARG D 38 67.438 −28.558 5.839 1.00 57.26 C ATOM 3141 NH1 ARG D 38 66.768 −27.415 5.974 1.00 56.27 N ATOM 3142 NH2 ARG D 38 68.751 −28.546 5.624 1.00 57.23 N ATOM 3143 C ARG D 38 62.090 −27.458 6.088 1.00 42.91 C ATOM 3144 O ARG D 38 62.281 −26.267 6.405 1.00 42.55 O ATOM 3145 N THR D 39 61.471 −28.341 6.874 1.00 42.58 N ATOM 3146 CA THR D 39 61.179 −28.177 8.299 1.00 41.28 C ATOM 3147 CB THR D 39 59.656 −28.312 8.600 1.00 41.27 C ATOM 3148 OG1 THR D 39 58.892 −27.440 7.743 1.00 43.39 O ATOM 3149 CG2 THR D 39 59.344 −27.965 10.027 1.00 42.59 C ATOM 3150 C THR D 39 61.989 −29.229 9.060 1.00 41.19 C ATOM 3151 O THR D 39 61.748 −30.449 8.968 1.00 40.45 O ATOM 3152 N LYS D 40 62.968 −28.750 9.804 1.00 40.73 N ATOM 3153 CA LYS D 40 63.868 −29.605 10.541 1.00 41.06 C ATOM 3154 CB LYS D 40 64.893 −28.753 11.289 1.00 41.28 C ATOM 3155 CG LYS D 40 66.298 −29.293 11.229 1.00 45.60 C ATOM 3156 CD LYS D 40 67.141 −28.840 12.503 1.00 49.44 C ATOM 3157 CE LYS D 40 68.173 −29.941 12.917 1.00 47.27 C ATOM 3158 NZ LYS D 40 68.965 −29.678 14.177 1.00 50.09 N ATOM 3159 C LYS D 40 63.075 −30.457 11.539 1.00 41.44 C ATOM 3160 O LYS D 40 62.069 −30.038 12.073 1.00 40.57 O ATOM 3161 N LEU D 41 63.524 −31.676 11.782 1.00 41.67 N ATOM 3162 CA LEU D 41 62.755 −32.533 12.643 1.00 42.41 C ATOM 3163 CB LEU D 41 63.321 −33.947 12.570 1.00 41.48 C ATOM 3164 CG LEU D 41 62.834 −34.954 13.562 1.00 42.23 C ATOM 3165 CD1 LEU D 41 63.555 −36.244 13.284 1.00 38.77 C ATOM 3166 CD2 LEU D 41 61.360 −35.124 13.379 1.00 42.31 C ATOM 3167 C LEU D 41 62.723 −31.942 14.067 1.00 42.92 C ATOM 3168 O LEU D 41 63.747 −31.819 14.744 1.00 42.91 O ATOM 3169 N GLY D 42 61.531 −31.532 14.484 1.00 43.29 N ATOM 3170 CA GLY D 42 61.306 −31.127 15.848 1.00 44.22 C ATOM 3171 C GLY D 42 61.080 −29.639 15.878 1.00 45.23 C ATOM 3172 O GLY D 42 60.854 −29.079 16.923 1.00 45.24 O ATOM 3173 N SER D 43 61.155 −29.018 14.704 1.00 46.01 N ATOM 3174 CA SER D 43 60.973 −27.595 14.531 1.00 47.24 C ATOM 3175 CB SER D 43 62.214 −27.065 13.803 1.00 46.38 C ATOM 3176 OG SER D 43 61.967 −25.912 13.064 1.00 48.60 O ATOM 3177 C SER D 43 59.635 −27.315 13.798 1.00 48.54 C ATOM 3178 O SER D 43 59.126 −28.181 13.090 1.00 48.74 O ATOM 3179 N THR D 44 59.057 −26.130 13.995 1.00 50.34 N ATOM 3180 CA THR D 44 57.829 −25.713 13.289 1.00 52.56 C ATOM 3181 CB THR D 44 56.759 −25.084 14.274 1.00 53.48 C ATOM 3182 OG1 THR D 44 56.875 −25.640 15.613 1.00 52.17 O ATOM 3183 CG2 THR D 44 55.331 −25.334 13.742 1.00 54.43 C ATOM 3184 C THR D 44 58.044 −24.766 12.057 1.00 54.01 C ATOM 3185 O THR D 44 57.128 −24.557 11.228 1.00 54.29 O ATOM 3186 N ASN D 45 59.246 −24.208 11.908 1.00 54.74 N ATOM 3187 CA ASN D 45 59.508 −23.303 10.784 1.00 55.53 C ATOM 3188 CB ASN D 45 60.529 −22.227 11.169 1.00 56.24 C ATOM 3189 CG ASN D 45 61.816 −22.827 11.744 1.00 59.18 C ATOM 3190 OD1 ASN D 45 62.441 −23.684 11.108 1.00 63.33 O ATOM 3191 ND2 ASN D 45 62.210 −22.391 12.954 1.00 59.01 N ATOM 3192 C ASN D 45 59.965 −24.043 9.524 1.00 55.48 C ATOM 3193 O ASN D 45 60.900 −24.875 9.572 1.00 55.04 O ATOM 3194 N GLU D 46 59.292 −23.739 8.413 1.00 55.16 N ATOM 3195 CA GLU D 46 59.654 −24.237 7.120 1.00 55.65 C ATOM 3196 CB GLU D 46 58.413 −24.405 6.238 1.00 56.04 C ATOM 3197 CG GLU D 46 58.708 −25.157 4.911 1.00 56.84 C ATOM 3198 CD GLU D 46 57.527 −25.197 3.937 1.00 58.64 C ATOM 3199 OE1 GLU D 46 57.030 −26.309 3.624 1.00 64.99 O ATOM 3200 OE2 GLU D 46 57.106 −24.115 3.448 1.00 64.43 O ATOM 3201 C GLU D 46 60.613 −23.246 6.494 1.00 54.79 C ATOM 3202 O GLU D 46 60.260 −22.103 6.253 1.00 55.34 O ATOM 3203 N GLN D 47 61.827 −23.695 6.233 1.00 53.79 N ATOM 3204 CA GLN D 47 62.853 −22.868 5.641 1.00 52.99 C ATOM 3205 CB GLN D 47 64.145 −23.017 6.442 1.00 53.28 C ATOM 3206 CG GLN D 47 64.900 −21.697 6.634 1.00 57.45 C ATOM 3207 CD GLN D 47 64.465 −20.874 7.888 1.00 59.69 C ATOM 3208 OE1 GLN D 47 65.207 −19.989 8.343 1.00 58.09 O ATOM 3209 NE2 GLN D 47 63.291 −21.193 8.452 1.00 61.05 N ATOM 3210 C GLN D 47 63.105 −23.262 4.184 1.00 51.77 C ATOM 3211 O GLN D 47 63.009 −24.438 3.832 1.00 50.62 O ATOM 3212 N SER D 48 63.439 −22.274 3.341 1.00 50.27 N ATOM 3213 CA SER D 48 63.767 −22.526 1.941 1.00 49.06 C ATOM 3214 CB SER D 48 63.715 −21.209 1.153 1.00 50.37 C ATOM 3215 OG SER D 48 62.799 −20.303 1.782 1.00 54.39 O ATOM 3216 C SER D 48 65.158 −23.135 1.844 1.00 46.80 C ATOM 3217 O SER D 48 66.000 −22.874 2.670 1.00 46.24 O ATOM 3218 N ILE D 49 65.401 −23.952 0.838 1.00 46.02 N ATOM 3219 CA ILE D 49 66.723 −24.566 0.630 1.00 45.76 C ATOM 3220 CB ILE D 49 66.583 −26.054 0.296 1.00 45.49 C ATOM 3221 CG1 ILE D 49 66.175 −26.853 1.553 1.00 44.65 C ATOM 3222 CD1 ILE D 49 65.438 −28.191 1.239 1.00 45.72 C ATOM 3223 CG2 ILE D 49 67.837 −26.618 −0.311 1.00 45.66 C ATOM 3224 C ILE D 49 67.497 −23.813 −0.475 1.00 46.86 C ATOM 3225 O ILE D 49 66.993 −23.579 −1.580 1.00 46.20 O ATOM 3226 N SER D 50 68.714 −23.400 −0.154 1.00 48.31 N ATOM 3227 CA SER D 50 69.582 −22.795 −1.161 1.00 50.07 C ATOM 3228 CB SER D 50 70.610 −21.875 −0.521 1.00 49.69 C ATOM 3229 OG SER D 50 69.966 −20.656 −0.222 1.00 51.30 O ATOM 3230 C SER D 50 70.259 −23.905 −1.918 1.00 50.54 C ATOM 3231 O SER D 50 70.853 −24.804 −1.304 1.00 50.91 O ATOM 3232 N ILE D 51 70.136 −23.854 −3.247 1.00 51.03 N ATOM 3233 CA ILE D 51 70.803 −24.826 −4.120 1.00 50.47 C ATOM 3234 CB ILE D 51 70.134 −24.926 −5.529 1.00 50.18 C ATOM 3235 CG1 ILE D 51 68.659 −25.348 −5.394 1.00 49.97 C ATOM 3236 CD1 ILE D 51 68.424 −26.692 −4.703 1.00 47.26 C ATOM 3237 CG2 ILE D 51 70.886 −25.890 −6.438 1.00 50.01 C ATOM 3238 C ILE D 51 72.267 −24.464 −4.162 1.00 50.13 C ATOM 3239 O ILE D 51 72.621 −23.304 −4.390 1.00 51.21 O ATOM 3240 N GLY D 52 73.112 −25.450 −3.903 1.00 49.83 N ATOM 3241 CA GLY D 52 74.537 −25.220 −3.804 1.00 49.62 C ATOM 3242 C GLY D 52 75.198 −26.276 −2.957 1.00 49.66 C ATOM 3243 O GLY D 52 74.639 −26.711 −1.948 1.00 50.36 O ATOM 3244 N GLY D 53 76.371 −26.698 −3.407 1.00 49.38 N ATOM 3245 CA GLY D 53 77.253 −27.612 −2.696 1.00 49.23 C ATOM 3246 C GLY D 53 76.697 −29.008 −2.480 1.00 49.36 C ATOM 3247 O GLY D 53 76.756 −29.935 −3.362 1.00 49.29 O ATOM 3248 N ARG D 54 76.120 −29.151 −1.269 1.00 49.43 N ATOM 3249 CA ARG D 54 75.465 −30.394 −0.907 1.00 49.74 C ATOM 3250 CB ARG D 54 75.282 −30.480 0.624 1.00 49.32 C ATOM 3251 CG ARG D 54 76.280 −31.418 1.274 1.00 50.69 C ATOM 3252 CD ARG D 54 76.661 −31.101 2.722 1.00 50.07 C ATOM 3253 NE ARG D 54 75.585 −30.643 3.597 1.00 48.37 N ATOM 3254 CZ ARG D 54 74.591 −31.392 4.086 1.00 49.71 C ATOM 3255 NH1 ARG D 54 74.447 −32.683 3.773 1.00 49.71 N ATOM 3256 NH2 ARG D 54 73.710 −30.832 4.899 1.00 47.05 N ATOM 3257 C ARG D 54 74.141 −30.581 −1.660 1.00 49.58 C ATOM 3258 O ARG D 54 73.723 −31.708 −1.911 1.00 50.26 O ATOM 3259 N TYR D 55 73.485 −29.486 −2.017 1.00 49.51 N ATOM 3260 CA TYR D 55 72.126 −29.555 −2.579 1.00 49.79 C ATOM 3261 CB TYR D 55 71.193 −28.546 −1.877 1.00 49.87 C ATOM 3262 CG TYR D 55 71.207 −28.685 −0.366 1.00 50.16 C ATOM 3263 CD1 TYR D 55 72.286 −28.218 0.368 1.00 50.07 C ATOM 3264 CE1 TYR D 55 72.336 −28.353 1.725 1.00 51.90 C ATOM 3265 CZ TYR D 55 71.290 −28.965 2.417 1.00 52.02 C ATOM 3266 OH TYR D 55 71.409 −29.070 3.799 1.00 51.10 O ATOM 3267 CE2 TYR D 55 70.183 −29.449 1.720 1.00 50.23 C ATOM 3268 CD2 TYR D 55 70.158 −29.306 0.317 1.00 48.86 C ATOM 3269 C TYR D 55 72.155 −29.335 −4.089 1.00 49.96 C ATOM 3270 O TYR D 55 72.233 −28.193 −4.549 1.00 49.02 O ATOM 3271 N VAL D 56 72.139 −30.445 −4.840 1.00 50.10 N ATOM 3272 CA VAL D 56 72.158 −30.378 −6.319 1.00 50.02 C ATOM 3273 CB VAL D 56 73.128 −31.484 −6.945 1.00 49.66 C ATOM 3274 CG1 VAL D 56 72.672 −31.803 −8.492 1.00 49.55 C ATOM 3275 CG2 VAL D 56 74.716 −31.073 −6.641 1.00 50.23 C ATOM 3276 C VAL D 56 70.703 −30.509 −6.834 1.00 50.01 C ATOM 3277 O VAL D 56 69.996 −31.474 −6.542 1.00 50.57 O ATOM 3278 N GLU D 57 70.240 −29.514 −7.565 1.00 50.47 N ATOM 3279 CA GLU D 57 68.959 −29.637 −8.261 1.00 50.96 C ATOM 3280 CB GLU D 57 68.069 −28.432 −8.002 1.00 49.91 C ATOM 3281 CG GLU D 57 66.785 −28.464 −8.792 1.00 48.91 C ATOM 3282 CD GLU D 57 65.896 −27.281 −8.499 1.00 46.98 C ATOM 3283 OE1 GLU D 57 66.400 −26.213 −8.111 1.00 46.14 O ATOM 3284 OE2 GLU D 57 64.670 −27.425 −8.644 1.00 49.35 O ATOM 3285 C GLU D 57 69.192 −29.777 −9.755 1.00 51.88 C ATOM 3286 O GLU D 57 70.071 −29.125 −10.302 1.00 52.11 O ATOM 3287 N THR D 58 68.414 −30.645 −10.396 1.00 53.11 N ATOM 3288 CA THR D 58 68.383 −30.727 −11.854 1.00 54.42 C ATOM 3289 CB THR D 58 69.137 −31.978 −12.403 1.00 54.38 C ATOM 3290 OG1 THR D 58 68.449 −33.205 −11.829 1.00 56.17 O ATOM 3291 CG2 THR D 58 70.734 −31.924 −12.037 1.00 55.32 C ATOM 3292 C THR D 58 66.896 −30.691 −12.250 1.00 55.02 C ATOM 3293 O THR D 58 66.072 −31.406 −11.670 1.00 55.11 O ATOM 3294 N VAL D 59 66.577 −29.813 −13.219 1.00 55.68 N ATOM 3295 CA VAL D 59 65.203 −29.468 −13.615 1.00 55.90 C ATOM 3296 CB VAL D 59 64.926 −27.955 −13.378 1.00 55.61 C ATOM 3297 CG1 VAL D 59 64.629 −27.687 −11.961 1.00 55.58 C ATOM 3298 CG2 VAL D 59 66.144 −27.115 −13.745 1.00 57.13 C ATOM 3299 C VAL D 59 64.991 −29.817 −15.100 1.00 56.39 C ATOM 3300 O VAL D 59 65.863 −29.553 −15.950 1.00 55.93 O ATOM 3301 N ASN D 60 63.840 −30.415 −15.410 1.00 56.80 N ATOM 3302 CA ASN D 60 63.549 −30.882 −16.774 1.00 56.63 C ATOM 3303 CB ASN D 60 63.691 −32.413 −16.873 1.00 56.38 C ATOM 3304 CG ASN D 60 64.099 −32.854 −18.348 1.00 57.37 C ATOM 3305 OD1 ASN D 60 65.090 −33.646 −18.466 1.00 56.92 O ATOM 3306 ND2 ASN D 60 63.351 −32.354 −19.408 1.00 55.67 N ATOM 3307 C ASN D 60 62.172 −30.461 −17.310 1.00 56.88 C ATOM 3308 O ASN D 60 61.252 −31.423 −17.192 1.00 56.87 O ATOM 3309 N LYS D 61 62.032 −28.997 −17.392 1.00 57.33 N ATOM 3310 CA LYS D 61 60.747 −28.473 −17.883 1.00 57.81 C ATOM 3311 CB LYS D 61 60.891 −26.968 −18.145 1.00 58.40 C ATOM 3312 CG LYS D 61 59.597 −26.259 −18.597 1.00 59.54 C ATOM 3313 CD LYS D 61 59.929 −25.060 −19.492 1.00 61.86 C ATOM 3314 CE LYS D 61 58.690 −24.361 −20.096 1.00 61.96 C ATOM 3315 NZ LYS D 61 58.446 −23.001 −19.525 1.00 62.65 N ATOM 3316 C LYS D 61 60.212 −29.215 −19.141 1.00 57.89 C ATOM 3317 O LYS D 61 58.997 −29.366 −19.309 1.00 58.21 O ATOM 3318 N GLY D 62 61.122 −29.693 −20.002 1.00 57.58 N ATOM 3319 CA GLY D 62 60.761 −30.486 −21.186 1.00 57.06 C ATOM 3320 C GLY D 62 60.000 −31.791 −20.907 1.00 56.82 C ATOM 3321 O GLY D 62 59.381 −32.386 −21.864 1.00 57.25 O ATOM 3322 N SER D 63 60.060 −32.244 −19.594 1.00 55.97 N ATOM 3323 CA SER D 63 59.302 −33.409 −19.125 1.00 54.90 C ATOM 3324 CB SER D 63 60.272 −34.621 −18.908 1.00 55.09 C ATOM 3325 OG SER D 63 60.645 −34.692 −17.338 1.00 54.74 O ATOM 3326 C SER D 63 58.474 −33.104 −17.762 1.00 53.75 C ATOM 3327 O SER D 63 57.786 −34.003 −17.034 1.00 53.64 O ATOM 3328 N LYS D 64 58.533 −31.834 −17.394 1.00 52.95 N ATOM 3329 CA LYS D 64 57.857 −31.310 −16.167 1.00 52.47 C ATOM 3330 CB LYS D 64 56.344 −31.240 −16.372 1.00 52.40 C ATOM 3331 CG LYS D 64 55.971 −29.890 −17.112 1.00 53.07 C ATOM 3332 CD LYS D 64 54.977 −30.113 −18.294 1.00 53.84 C ATOM 3333 CE LYS D 64 53.558 −30.322 −17.603 1.00 53.96 C ATOM 3334 NZ LYS D 64 52.517 −30.001 −18.618 1.00 51.87 N ATOM 3335 C LYS D 64 58.301 −31.907 −14.795 1.00 51.17 C ATOM 3336 O LYS D 64 57.603 −31.826 −13.761 1.00 51.55 O ATOM 3337 N SER D 65 59.517 −32.439 −14.827 1.00 49.79 N ATOM 3338 CA SER D 65 60.167 −33.103 −13.708 1.00 49.92 C ATOM 3339 CB SER D 65 60.834 −34.407 −14.213 1.00 49.55 C ATOM 3340 OG SER D 65 61.759 −34.932 −13.248 1.00 53.24 O ATOM 3341 C SER D 65 61.234 −32.168 −13.120 1.00 49.16 C ATOM 3342 O SER D 65 61.838 −31.333 −13.866 1.00 48.96 O ATOM 3343 N PHE D 66 61.437 −32.304 −11.802 1.00 47.24 N ATOM 3344 CA PHE D 66 62.543 −31.670 −11.066 1.00 46.15 C ATOM 3345 CB PHE D 66 62.277 −30.171 −10.826 1.00 44.90 C ATOM 3346 CG PHE D 66 61.128 −29.867 −9.891 1.00 44.59 C ATOM 3347 CD1 PHE D 66 59.801 −29.989 −10.317 1.00 42.09 C ATOM 3348 CE1 PHE D 66 58.738 −29.686 −9.470 1.00 41.74 C ATOM 3349 CZ PHE D 66 58.997 −29.224 −8.170 1.00 42.61 C ATOM 3350 CE2 PHE D 66 60.315 −29.087 −7.722 1.00 43.21 C ATOM 3351 CD2 PHE D 66 61.376 −29.410 −8.586 1.00 44.86 C ATOM 3352 C PHE D 66 62.988 −32.439 −9.769 1.00 45.82 C ATOM 3353 O PHE D 66 62.222 −33.197 −9.181 1.00 46.26 O ATOM 3354 N SER D 67 64.238 −32.257 −9.351 1.00 45.70 N ATOM 3355 CA SER D 67 64.862 −33.149 −8.367 1.00 45.45 C ATOM 3356 CB SER D 67 65.603 −34.242 −9.113 1.00 45.90 C ATOM 3357 OG SER D 67 64.734 −35.335 −9.256 1.00 47.19 O ATOM 3358 C SER D 67 65.871 −32.497 −7.455 1.00 45.20 C ATOM 3359 O SER D 67 66.655 −31.642 −7.902 1.00 46.01 O ATOM 3360 N LEU D 68 65.872 −32.930 −6.196 1.00 44.54 N ATOM 3361 CA LEU D 68 66.855 −32.507 −5.212 1.00 44.12 C ATOM 3362 CB LEU D 68 66.203 −31.902 −3.968 1.00 43.76 C ATOM 3363 CG LEU D 68 66.799 −30.640 −3.315 1.00 44.66 C ATOM 3364 CD1 LEU D 68 66.693 −30.684 −1.812 1.00 45.00 C ATOM 3365 CD2 LEU D 68 68.213 −30.336 −3.739 1.00 41.15 C ATOM 3366 C LEU D 68 67.653 −33.717 −4.766 1.00 43.76 C ATOM 3367 O LEU D 68 67.095 −34.701 −4.302 1.00 41.85 O ATOM 3368 N ARG D 69 68.966 −33.629 −4.920 1.00 44.26 N ATOM 3369 CA ARG D 69 69.873 −34.621 −4.383 1.00 45.51 C ATOM 3370 CB ARG D 69 70.817 −35.147 −5.493 1.00 44.78 C ATOM 3371 CG ARG D 69 71.578 −36.356 −5.011 1.00 47.38 C ATOM 3372 CD ARG D 69 72.519 −36.978 −6.039 1.00 50.01 C ATOM 3373 NE ARG D 69 73.038 −38.236 −5.447 1.00 64.56 N ATOM 3374 CZ ARG D 69 74.278 −38.371 −4.916 1.00 70.54 C ATOM 3375 NH1 ARG D 69 75.200 −37.308 −4.958 1.00 70.65 N ATOM 3376 NH2 ARG D 69 74.628 −39.585 −4.368 1.00 70.40 N ATOM 3377 C ARG D 69 70.647 −33.877 −3.316 1.00 44.18 C ATOM 3378 O ARG D 69 71.228 −32.821 −3.583 1.00 45.88 O ATOM 3379 N ILE D 70 70.611 −34.393 −2.100 1.00 44.15 N ATOM 3380 CA ILE D 70 71.400 −33.865 −1.004 1.00 43.11 C ATOM 3381 CB ILE D 70 70.560 −33.577 0.247 1.00 43.37 C ATOM 3382 CG1 ILE D 70 69.343 −32.713 −0.092 1.00 40.96 C ATOM 3383 CD1 ILE D 70 68.184 −33.028 0.730 1.00 43.95 C ATOM 3384 CG2 ILE D 70 71.443 −32.879 1.306 1.00 43.28 C ATOM 3385 C ILE D 70 72.431 −34.947 −0.699 1.00 43.35 C ATOM 3386 O ILE D 70 72.072 −36.079 −0.404 1.00 42.77 O ATOM 3387 N SER D 71 73.707 −34.619 −0.851 1.00 43.10 N ATOM 3388 CA SER D 71 74.735 −35.597 −0.571 1.00 43.65 C ATOM 3389 CB SER D 71 75.794 −35.590 −1.669 1.00 43.42 C ATOM 3390 OG SER D 71 76.168 −34.259 −1.929 1.00 44.36 O ATOM 3391 C SER D 71 75.306 −35.317 0.817 1.00 43.63 C ATOM 3392 O SER D 71 74.923 −34.309 1.447 1.00 44.14 O ATOM 3393 N ASP D 72 76.156 −36.232 1.309 1.00 43.29 N ATOM 3394 CA ASP D 72 76.858 −36.065 2.582 1.00 42.35 C ATOM 3395 CB ASP D 72 77.912 −34.951 2.458 1.00 42.24 C ATOM 3396 CG ASP D 72 78.973 −35.012 3.572 1.00 44.75 C ATOM 3397 OD1 ASP D 72 78.995 −36.012 4.344 1.00 42.13 O ATOM 3398 OD2 ASP D 72 79.800 −34.057 3.659 1.00 47.88 O ATOM 3399 C ASP D 72 75.880 −35.777 3.746 1.00 41.01 C ATOM 3400 O ASP D 72 75.935 −34.731 4.394 1.00 40.46 O ATOM 3401 N LEU D 73 74.982 −36.713 4.003 1.00 40.43 N ATOM 3402 CA LEU D 73 73.915 −36.470 4.965 1.00 39.98 C ATOM 3403 CB LEU D 73 72.761 −37.447 4.752 1.00 40.03 C ATOM 3404 CG LEU D 73 71.891 −37.260 3.493 1.00 38.61 C ATOM 3405 CD1 LEU D 73 70.971 −38.462 3.446 1.00 37.16 C ATOM 3406 CD2 LEU D 73 71.094 −36.006 3.576 1.00 38.44 C ATOM 3407 C LEU D 73 74.409 −36.458 6.424 1.00 39.77 C ATOM 3408 O LEU D 73 75.344 −37.149 6.802 1.00 38.86 O ATOM 3409 N ARG D 74 73.784 −35.600 7.214 1.00 40.34 N ATOM 3410 CA ARG D 74 74.125 −35.418 8.616 1.00 40.91 C ATOM 3411 CB ARG D 74 74.711 −34.024 8.803 1.00 41.22 C ATOM 3412 CG ARG D 74 75.561 −33.574 7.623 1.00 44.83 C ATOM 3413 CD ARG D 74 76.259 −32.276 7.888 1.00 51.37 C ATOM 3414 NE ARG D 74 75.309 −31.193 8.146 1.00 55.28 N ATOM 3415 CZ ARG D 74 75.645 −30.008 8.662 1.00 56.79 C ATOM 3416 NH1 ARG D 74 76.913 −29.758 8.987 1.00 55.96 N ATOM 3417 NH2 ARG D 74 74.711 −29.079 8.868 1.00 56.56 N ATOM 3418 C ARG D 74 72.820 −35.563 9.406 1.00 40.45 C ATOM 3419 O ARG D 74 71.735 −35.292 8.851 1.00 40.13 O ATOM 3420 N VAL D 75 72.901 −36.003 10.663 1.00 39.63 N ATOM 3421 CA VAL D 75 71.700 −36.030 11.512 1.00 40.06 C ATOM 3422 CB VAL D 75 71.970 −36.527 12.963 1.00 39.68 C ATOM 3423 CG1 VAL D 75 72.504 −37.923 12.939 1.00 37.56 C ATOM 3424 CG2 VAL D 75 72.893 −35.615 13.685 1.00 41.38 C ATOM 3425 C VAL D 75 70.872 −34.702 11.509 1.00 40.03 C ATOM 3426 O VAL D 75 69.652 −34.750 11.502 1.00 40.31 O ATOM 3427 N GLU D 76 71.516 −33.534 11.474 1.00 39.38 N ATOM 3428 CA GLU D 76 70.783 −32.267 11.413 1.00 38.58 C ATOM 3429 CB GLU D 76 71.704 −31.072 11.643 1.00 39.43 C ATOM 3430 CG GLU D 76 73.155 −31.300 11.253 1.00 43.81 C ATOM 3431 CD GLU D 76 73.899 −32.091 12.300 1.00 49.07 C ATOM 3432 OE1 GLU D 76 74.410 −33.201 12.002 1.00 50.38 O ATOM 3433 OE2 GLU D 76 73.963 −31.604 13.445 1.00 53.73 O ATOM 3434 C GLU D 76 70.012 −32.038 10.113 1.00 37.13 C ATOM 3435 O GLU D 76 69.328 −31.018 9.981 1.00 36.46 O ATOM 3436 N ASP D 77 70.139 −32.955 9.156 1.00 35.88 N ATOM 3437 CA ASP D 77 69.302 −32.934 7.896 1.00 35.98 C ATOM 3438 CB ASP D 77 69.995 −33.640 6.719 1.00 35.29 C ATOM 3439 CG ASP D 77 71.259 −32.944 6.258 1.00 36.12 C ATOM 3440 OD1 ASP D 77 71.314 −31.707 6.247 1.00 34.87 O ATOM 3441 OD2 ASP D 77 72.200 −33.674 5.890 1.00 39.60 O ATOM 3442 C ASP D 77 67.933 −33.626 8.022 1.00 35.40 C ATOM 3443 O ASP D 77 67.106 −33.451 7.146 1.00 35.70 O ATOM 3444 N SER D 78 67.740 −34.480 9.027 1.00 34.77 N ATOM 3445 CA SER D 78 66.422 −34.981 9.345 1.00 35.45 C ATOM 3446 CB SER D 78 66.473 −35.750 10.659 1.00 35.78 C ATOM 3447 OG SER D 78 67.436 −36.770 10.546 1.00 36.74 O ATOM 3448 C SER D 78 65.321 −33.899 9.393 1.00 35.23 C ATOM 3449 O SER D 78 65.471 −32.828 10.038 1.00 35.34 O ATOM 3450 N GLY D 79 64.210 −34.192 8.716 1.00 33.82 N ATOM 3451 CA GLY D 79 63.078 −33.271 8.649 1.00 34.33 C ATOM 3452 C GLY D 79 62.191 −33.603 7.481 1.00 35.45 C ATOM 3453 O GLY D 79 62.404 −34.627 6.767 1.00 36.59 O ATOM 3454 N THR D 80 61.239 −32.707 7.242 1.00 36.95 N ATOM 3455 CA THR D 80 60.265 −32.773 6.142 1.00 37.81 C ATOM 3456 CB THR D 80 58.812 −32.455 6.589 1.00 37.21 C ATOM 3457 OG1 THR D 80 58.540 −33.092 7.845 1.00 42.51 O ATOM 3458 CG2 THR D 80 57.794 −32.957 5.599 1.00 36.93 C ATOM 3459 C THR D 80 60.658 −31.822 5.030 1.00 39.38 C ATOM 3460 O THR D 80 60.734 −30.616 5.253 1.00 39.45 O ATOM 3461 N TYR D 81 60.882 −32.394 3.835 1.00 39.69 N ATOM 3462 CA TYR D 81 61.244 −31.683 2.641 1.00 40.11 C ATOM 3463 CB TYR D 81 62.433 −32.367 1.967 1.00 40.22 C ATOM 3464 CG TYR D 81 63.719 −32.354 2.802 1.00 39.55 C ATOM 3465 CD1 TYR D 81 64.755 −31.515 2.468 1.00 39.29 C ATOM 3466 CE1 TYR D 81 65.935 −31.489 3.213 1.00 39.91 C ATOM 3467 CZ TYR D 81 66.087 −32.315 4.305 1.00 40.52 C ATOM 3468 OH TYR D 81 67.291 −32.242 5.010 1.00 39.06 O ATOM 3469 CE2 TYR D 81 65.066 −33.175 4.655 1.00 37.99 C ATOM 3470 CD2 TYR D 81 63.892 −33.194 3.897 1.00 38.47 C ATOM 3471 C TYR D 81 60.064 −31.621 1.693 1.00 40.88 C ATOM 3472 O TYR D 81 59.242 −32.572 1.577 1.00 42.06 O ATOM 3473 N LYS D 82 59.925 −30.469 1.063 1.00 41.23 N ATOM 3474 CA LYS D 82 58.819 −30.189 0.172 1.00 41.95 C ATOM 3475 CB LYS D 82 57.779 −29.315 0.863 1.00 42.23 C ATOM 3476 CG LYS D 82 56.447 −30.008 1.156 1.00 46.06 C ATOM 3477 CD LYS D 82 55.949 −29.607 2.549 1.00 53.37 C ATOM 3478 CE LYS D 82 54.875 −30.528 3.091 1.00 51.30 C ATOM 3479 NZ LYS D 82 53.540 −30.122 2.613 1.00 50.40 N ATOM 3480 C LYS D 82 59.381 −29.472 −1.028 1.00 42.24 C ATOM 3481 O LYS D 82 60.236 −28.607 −0.899 1.00 41.51 O ATOM 3482 N CYS D 83 58.912 −29.863 −2.207 1.00 43.47 N ATOM 3483 CA CYS D 83 59.163 −29.117 −3.400 1.00 44.82 C ATOM 3484 CB CYS D 83 59.474 −30.038 −4.564 1.00 45.49 C ATOM 3485 SG CYS D 83 58.161 −31.141 −4.953 1.00 44.99 S ATOM 3486 C CYS D 83 57.923 −28.295 −3.711 1.00 45.88 C ATOM 3487 O CYS D 83 56.827 −28.610 −3.259 1.00 46.33 O ATOM 3488 N GLN D 84 58.132 −27.220 −4.465 1.00 46.29 N ATOM 3489 CA GLN D 84 57.058 −26.400 −5.007 1.00 45.80 C ATOM 3490 CB GLN D 84 56.949 −25.084 −4.280 1.00 46.07 C ATOM 3491 CG GLN D 84 55.811 −24.290 −4.826 1.00 47.89 C ATOM 3492 CD GLN D 84 55.202 −23.369 −3.835 1.00 50.52 C ATOM 3493 OE1 GLN D 84 54.030 −23.056 −3.953 1.00 54.26 O ATOM 3494 NE2 GLN D 84 55.991 −22.898 −2.861 1.00 50.71 N ATOM 3495 C GLN D 84 57.352 −26.107 −6.466 1.00 44.92 C ATOM 3496 O GLN D 84 58.466 −25.756 −6.822 1.00 44.76 O ATOM 3497 N ALA D 85 56.328 −26.309 −7.271 1.00 44.45 N ATOM 3498 CA ALA D 85 56.287 −26.074 −8.693 1.00 44.03 C ATOM 3499 CB ALA D 85 55.513 −27.178 −9.330 1.00 43.73 C ATOM 3500 C ALA D 85 55.581 −24.740 −8.953 1.00 44.64 C ATOM 3501 O ALA D 85 54.506 −24.480 −8.398 1.00 45.56 O ATOM 3502 N PHE D 86 56.179 −23.900 −9.797 1.00 44.70 N ATOM 3503 CA PHE D 86 55.646 −22.570 −10.110 1.00 43.77 C ATOM 3504 CB PHE D 86 56.662 −21.505 −9.755 1.00 43.68 C ATOM 3505 CG PHE D 86 56.899 −21.325 −8.234 1.00 43.64 C ATOM 3506 CD1 PHE D 86 58.108 −21.734 −7.644 1.00 39.50 C ATOM 3507 CE1 PHE D 86 58.352 −21.536 −6.258 1.00 41.98 C ATOM 3508 CZ PHE D 86 57.392 −20.906 −5.466 1.00 43.10 C ATOM 3509 CE2 PHE D 86 56.164 −20.469 −6.060 1.00 42.82 C ATOM 3510 CD2 PHE D 86 55.936 −20.693 −7.427 1.00 42.57 C ATOM 3511 C PHE D 86 55.284 −22.518 −11.581 1.00 43.35 C ATOM 3512 O PHE D 86 56.047 −22.948 −12.451 1.00 43.61 O ATOM 3513 N TYR D 87 54.071 −22.067 −11.860 1.00 43.20 N ATOM 3514 CA TYR D 87 53.528 −22.118 −13.225 1.00 42.85 C ATOM 3515 CB TYR D 87 52.706 −23.392 −13.419 1.00 42.88 C ATOM 3516 CG TYR D 87 51.616 −23.570 −12.381 1.00 43.24 C ATOM 3517 CD1 TYR D 87 50.361 −23.023 −12.574 1.00 41.66 C ATOM 3518 CE1 TYR D 87 49.378 −23.166 −11.626 1.00 43.81 C ATOM 3519 CZ TYR D 87 49.645 −23.855 −10.456 1.00 42.83 C ATOM 3520 OH TYR D 87 48.635 −23.981 −9.495 1.00 45.90 O ATOM 3521 CE2 TYR D 87 50.879 −24.412 −10.260 1.00 40.71 C ATOM 3522 CD2 TYR D 87 51.849 −24.270 −11.203 1.00 41.31 C ATOM 3523 C TYR D 87 52.678 −20.887 −13.442 1.00 42.38 C ATOM 3524 O TYR D 87 52.341 −20.184 −12.479 1.00 41.90 O ATOM 3525 N VAL D 88 52.328 −20.625 −14.690 1.00 42.33 N ATOM 3526 CA VAL D 88 51.484 −19.482 −15.014 1.00 42.91 C ATOM 3527 CB VAL D 88 52.241 −18.322 −15.725 1.00 42.23 C ATOM 3528 CG1 VAL D 88 52.648 −18.693 −17.134 1.00 42.89 C ATOM 3529 CG2 VAL D 88 53.461 −17.852 −14.923 1.00 42.15 C ATOM 3530 C VAL D 88 50.343 −20.009 −15.861 1.00 43.65 C ATOM 3531 O VAL D 88 50.483 −21.016 −16.523 1.00 44.60 O ATOM 3532 N PHE D 89 49.204 −19.351 −15.789 1.00 44.07 N ATOM 3533 CA PHE D 89 48.019 −19.716 −16.558 1.00 44.21 C ATOM 3534 CB PHE D 89 47.186 −20.807 −15.865 1.00 43.34 C ATOM 3535 CG PHE D 89 46.719 −20.466 −14.459 1.00 42.59 C ATOM 3536 CD1 PHE D 89 45.427 −19.948 −14.236 1.00 42.34 C ATOM 3537 CE1 PHE D 89 44.978 −19.651 −12.942 1.00 41.00 C ATOM 3538 CZ PHE D 89 45.828 −19.873 −11.839 1.00 41.21 C ATOM 3539 CE2 PHE D 89 47.115 −20.389 −12.048 1.00 40.99 C ATOM 3540 CD2 PHE D 89 47.547 −20.683 −13.358 1.00 39.83 C ATOM 3541 C PHE D 89 47.258 −18.419 −16.699 1.00 45.29 C ATOM 3542 O PHE D 89 47.586 −17.446 −16.012 1.00 44.92 O ATOM 3543 N PHE D 90 46.278 −18.379 −17.594 1.00 46.60 N ATOM 3544 CA PHE D 90 45.525 −17.166 −17.790 1.00 47.84 C ATOM 3545 CB PHE D 90 45.113 −17.033 −19.229 1.00 49.12 C ATOM 3546 CG PHE D 90 46.217 −16.590 −20.135 1.00 52.21 C ATOM 3547 CD1 PHE D 90 46.291 −15.259 −20.561 1.00 55.64 C ATOM 3548 CE1 PHE D 90 47.315 −14.828 −21.443 1.00 57.08 C ATOM 3549 CZ PHE D 90 48.263 −15.751 −21.908 1.00 55.59 C ATOM 3550 CE2 PHE D 90 48.194 −17.095 −21.480 1.00 57.82 C ATOM 3551 CD2 PHE D 90 47.171 −17.503 −20.596 1.00 55.72 C ATOM 3552 C PHE D 90 44.331 −17.079 −16.865 1.00 47.66 C ATOM 3553 O PHE D 90 43.697 −18.071 −16.572 1.00 46.94 O ATOM 3554 N ALA D 91 44.053 −15.867 −16.398 1.00 48.49 N ATOM 3555 CA ALA D 91 42.982 −15.599 −15.447 1.00 49.73 C ATOM 3556 CB ALA D 91 42.942 −14.112 −15.129 1.00 48.83 C ATOM 3557 C ALA D 91 41.632 −16.093 −15.969 1.00 51.41 C ATOM 3558 O ALA D 91 40.799 −16.593 −15.209 1.00 51.12 O ATOM 3559 N GLU D 92 41.441 −15.964 −17.282 1.00 53.68 N ATOM 3560 CA GLU D 92 40.229 −16.427 −17.962 1.00 56.07 C ATOM 3561 CB GLU D 92 40.134 −15.798 −19.358 1.00 56.18 C ATOM 3562 CG GLU D 92 40.983 −16.517 −20.403 1.00 57.25 C ATOM 3563 CD GLU D 92 41.361 −15.626 −21.547 1.00 59.32 C ATOM 3564 OE1 GLU D 92 42.579 −15.479 −21.797 1.00 59.13 O ATOM 3565 OE2 GLU D 92 40.441 −15.065 −22.189 1.00 60.55 O ATOM 3566 C GLU D 92 40.105 −17.952 −18.095 1.00 57.18 C ATOM 3567 O GLU D 92 39.052 −18.416 −18.520 1.00 57.56 O ATOM 3568 N ASP D 93 41.171 −18.709 −17.789 1.00 58.82 N ATOM 3569 CA ASP D 93 41.110 −20.181 −17.684 1.00 60.41 C ATOM 3570 CB ASP D 93 42.458 −20.800 −17.271 1.00 60.06 C ATOM 3571 CG ASP D 93 42.370 −22.306 −16.993 1.00 62.32 C ATOM 3572 OD1 ASP D 93 43.088 −22.798 −16.075 1.00 63.69 O ATOM 3573 OD2 ASP D 93 41.580 −23.010 −17.680 1.00 63.08 O ATOM 3574 C ASP D 93 39.992 −20.523 −16.698 1.00 61.55 C ATOM 3575 O ASP D 93 40.234 −20.746 −15.495 1.00 61.84 O ATOM 3576 N VAL D 94 38.775 −20.549 −17.266 1.00 62.79 N ATOM 3577 CA VAL D 94 37.473 −20.563 −16.567 1.00 63.66 C ATOM 3578 CB VAL D 94 36.302 −20.047 −17.526 1.00 63.67 C ATOM 3579 CG1 VAL D 94 35.125 −19.424 −16.748 1.00 63.68 C ATOM 3580 CG2 VAL D 94 35.843 −21.115 −18.522 1.00 63.79 C ATOM 3581 C VAL D 94 37.238 −21.948 −15.970 1.00 64.13 C ATOM 3582 O VAL D 94 38.119 −22.810 −16.078 1.00 64.47 O ATOM 3583 N GLY D 95 36.089 −22.145 −15.317 1.00 64.40 N ATOM 3584 CA GLY D 95 35.774 −23.376 −14.568 1.00 64.71 C ATOM 3585 C GLY D 95 36.866 −24.412 −14.294 1.00 65.01 C ATOM 3586 O GLY D 95 36.569 −25.624 −14.258 1.00 65.10 O ATOM 3587 N SER D 96 38.110 −23.954 −14.083 1.00 65.03 N ATOM 3588 CA SER D 96 39.264 −24.858 −13.891 1.00 65.03 C ATOM 3589 CB SER D 96 40.390 −24.533 −14.887 1.00 65.25 C ATOM 3590 OG SER D 96 41.339 −25.594 −14.955 1.00 64.98 O ATOM 3591 C SER D 96 39.806 −24.852 −12.454 1.00 64.82 C ATOM 3592 O SER D 96 40.023 −23.779 −11.867 1.00 65.31 O ATOM 3593 N ASN D 97 40.052 −26.057 −11.928 1.00 63.87 N ATOM 3594 CA ASN D 97 40.392 −26.313 −10.521 1.00 62.98 C ATOM 3595 CB ASN D 97 39.702 −27.644 −10.104 1.00 63.42 C ATOM 3596 CG ASN D 97 39.953 −28.045 −8.633 1.00 65.04 C ATOM 3597 OD1 ASN D 97 40.047 −27.190 −7.736 1.00 66.76 O ATOM 3598 ND2 ASN D 97 40.030 −29.363 −8.387 1.00 63.43 N ATOM 3599 C ASN D 97 41.921 −26.317 −10.231 1.00 61.78 C ATOM 3600 O ASN D 97 42.552 −27.385 −10.142 1.00 61.83 O ATOM 3601 N LYS D 98 42.507 −25.129 −10.063 1.00 59.84 N ATOM 3602 CA LYS D 98 43.970 −24.994 −9.904 1.00 58.24 C ATOM 3603 CB LYS D 98 44.446 −23.620 −10.431 1.00 58.64 C ATOM 3604 CG LYS D 98 44.251 −23.361 −11.938 1.00 57.61 C ATOM 3605 CD LYS D 98 42.829 −22.926 −12.285 1.00 57.73 C ATOM 3606 CE LYS D 98 42.248 −21.834 −11.301 1.00 59.29 C ATOM 3607 NZ LYS D 98 41.046 −20.972 −12.134 1.00 57.74 N ATOM 3608 C LYS D 98 44.493 −25.245 −8.461 1.00 57.13 C ATOM 3609 O LYS D 98 43.767 −25.784 −7.606 1.00 57.08 O ATOM 3610 N GLY D 99 45.767 −24.891 −8.225 1.00 55.60 N ATOM 3611 CA GLY D 99 46.378 −24.754 −6.872 1.00 52.95 C ATOM 3612 C GLY D 99 46.501 −23.279 −6.415 1.00 50.67 C ATOM 3613 O GLY D 99 45.678 −22.440 −6.801 1.00 51.24 O ATOM 3614 N ALA D 100 47.510 −22.956 −5.601 1.00 47.56 N ATOM 3615 CA ALA D 100 47.594 −21.643 −4.932 1.00 44.47 C ATOM 3616 CB ALA D 100 48.583 −21.700 −3.781 1.00 44.23 C ATOM 3617 C ALA D 100 47.948 −20.493 −5.881 1.00 42.73 C ATOM 3618 O ALA D 100 48.733 −20.692 −6.805 1.00 41.87 O ATOM 3619 N ILE D 101 47.368 −19.313 −5.635 1.00 40.81 N ATOM 3620 CA ILE D 101 47.614 −18.108 −6.395 1.00 40.35 C ATOM 3621 CB ILE D 101 46.370 −17.176 −6.453 1.00 40.67 C ATOM 3622 CG1 ILE D 101 45.119 −17.901 −6.945 1.00 41.30 C ATOM 3623 CD1 ILE D 101 45.229 −18.533 −8.316 1.00 44.91 C ATOM 3624 CG2 ILE D 101 46.719 −15.835 −7.192 1.00 38.52 C ATOM 3625 C ILE D 101 48.703 −17.316 −5.677 1.00 40.37 C ATOM 3626 O ILE D 101 48.578 −17.042 −4.478 1.00 40.20 O ATOM 3627 N ILE D 102 49.757 −16.950 −6.405 1.00 39.73 N ATOM 3628 CA ILE D 102 50.891 −16.245 −5.850 1.00 38.51 C ATOM 3629 CB ILE D 102 52.225 −16.834 −6.388 1.00 39.69 C ATOM 3630 CG1 ILE D 102 52.294 −18.341 −6.159 1.00 40.45 C ATOM 3631 CD1 ILE D 102 52.156 −18.810 −4.677 1.00 39.56 C ATOM 3632 CG2 ILE D 102 53.461 −16.084 −5.804 1.00 40.43 C ATOM 3633 C ILE D 102 50.816 −14.788 −6.296 1.00 37.28 C ATOM 3634 O ILE D 102 51.315 −13.893 −5.613 1.00 38.01 O ATOM 3635 N GLY D 103 50.181 −14.539 −7.424 1.00 35.03 N ATOM 3636 CA GLY D 103 50.172 −13.194 −7.991 1.00 33.31 C ATOM 3637 C GLY D 103 49.411 −13.068 −9.275 1.00 32.34 C ATOM 3638 O GLY D 103 49.072 −14.050 −9.924 1.00 31.10 O ATOM 3639 N LEU D 104 49.098 −11.840 −9.621 1.00 32.17 N ATOM 3640 CA LEU D 104 48.403 −11.557 −10.841 1.00 32.15 C ATOM 3641 CB LEU D 104 46.965 −11.134 −10.534 1.00 33.36 C ATOM 3642 CG LEU D 104 46.100 −10.577 −11.696 1.00 35.07 C ATOM 3643 CD1 LEU D 104 44.837 −9.947 −11.110 1.00 35.43 C ATOM 3644 CD2 LEU D 104 45.772 −11.706 −12.740 1.00 34.01 C ATOM 3645 C LEU D 104 49.131 −10.472 −11.532 1.00 32.05 C ATOM 3646 O LEU D 104 49.436 −9.462 −10.903 1.00 31.50 O ATOM 3647 N MET D 105 49.419 −10.679 −12.826 1.00 31.71 N ATOM 3648 CA MET D 105 50.112 −9.717 −13.682 1.00 31.42 C ATOM 3649 CB MET D 105 51.206 −10.403 −14.533 1.00 31.83 C ATOM 3650 CG MET D 105 52.155 −11.228 −13.703 1.00 36.87 C ATOM 3651 SD MET D 105 53.267 −10.213 −12.674 1.00 43.45 S ATOM 3652 CE MET D 105 54.104 −9.296 −13.942 1.00 32.92 C ATOM 3653 C MET D 105 49.131 −9.055 −14.624 1.00 30.41 C ATOM 3654 O MET D 105 48.154 −9.673 −15.072 1.00 29.25 O ATOM 3655 N VAL D 106 49.362 −7.789 −14.917 1.00 29.43 N ATOM 3656 CA VAL D 106 48.394 −7.148 −15.760 1.00 30.76 C ATOM 3657 CB VAL D 106 48.317 −5.542 −15.699 1.00 30.85 C ATOM 3658 CG1 VAL D 106 48.876 −4.946 −14.421 1.00 28.68 C ATOM 3659 CG2 VAL D 106 48.867 −4.937 −16.875 1.00 27.85 C ATOM 3660 C VAL D 106 48.670 −7.711 −17.170 1.00 31.76 C ATOM 3661 O VAL D 106 49.843 −7.941 −17.524 1.00 32.26 O ATOM 3662 N GLY D 107 47.590 −7.909 −17.944 1.00 31.86 N ATOM 3663 CA GLY D 107 47.602 −8.730 −19.149 1.00 31.60 C ATOM 3664 C GLY D 107 46.937 −10.076 −18.867 1.00 31.76 C ATOM 3665 O GLY D 107 46.782 −10.884 −19.774 1.00 32.48 O ATOM 3666 N GLY D 108 46.594 −10.347 −17.602 1.00 31.73 N ATOM 3667 CA GLY D 108 45.845 −11.561 −17.219 1.00 30.76 C ATOM 3668 C GLY D 108 46.575 −12.837 −16.858 1.00 30.68 C ATOM 3669 O GLY D 108 45.940 −13.868 −16.709 1.00 31.60 O ATOM 3670 N VAL D 109 47.894 −12.799 −16.705 1.00 31.23 N ATOM 3671 CA VAL D 109 48.659 −14.009 −16.355 1.00 31.01 C ATOM 3672 CB VAL D 109 50.115 −13.935 −16.919 1.00 31.60 C ATOM 3673 CG1 VAL D 109 50.128 −14.044 −18.453 1.00 30.53 C ATOM 3674 CG2 VAL D 109 50.988 −14.970 −16.332 1.00 28.81 C ATOM 3675 C VAL D 109 48.653 −14.172 −14.835 1.00 32.20 C ATOM 3676 O VAL D 109 48.994 −13.258 −14.125 1.00 32.24 O ATOM 3677 N VAL D 110 48.207 −15.323 −14.332 1.00 33.52 N ATOM 3678 CA VAL D 110 48.274 −15.592 −12.911 1.00 34.03 C ATOM 3679 CB VAL D 110 46.863 −15.796 −12.233 1.00 34.35 C ATOM 3680 CG1 VAL D 110 46.831 −16.818 −11.135 1.00 33.72 C ATOM 3681 CG2 VAL D 110 45.754 −15.985 −13.234 1.00 34.18 C ATOM 3682 C VAL D 110 49.389 −16.575 −12.582 1.00 35.97 C ATOM 3683 O VAL D 110 49.627 −17.552 −13.306 1.00 35.08 O ATOM 3684 N ILE D 111 50.130 −16.253 −11.526 1.00 38.15 N ATOM 3685 CA ILE D 111 51.201 −17.117 −11.055 1.00 40.04 C ATOM 3686 CB ILE D 111 52.441 −16.328 −10.556 1.00 39.96 C ATOM 3687 CG1 ILE D 111 53.021 −15.546 −11.706 1.00 40.77 C ATOM 3688 CD1 ILE D 111 52.827 −14.083 −11.586 1.00 42.20 C ATOM 3689 CG2 ILE D 111 53.550 −17.273 −10.029 1.00 40.87 C ATOM 3690 C ILE D 111 50.628 −18.015 −10.003 1.00 40.99 C ATOM 3691 O ILE D 111 50.059 −17.563 −8.987 1.00 41.58 O ATOM 3692 N GLY D 112 50.722 −19.313 −10.257 1.00 42.26 N ATOM 3693 CA GLY D 112 50.331 −20.269 −9.235 1.00 41.93 C ATOM 3694 C GLY D 112 51.500 −21.086 −8.715 1.00 43.09 C ATOM 3695 O GLY D 112 52.575 −21.142 −9.325 1.00 42.76 O ATOM 3696 N GLY D 113 51.266 −21.778 −7.598 1.00 44.33 N ATOM 3697 CA GLY D 113 52.260 −22.648 −7.011 1.00 45.49 C ATOM 3698 C GLY D 113 51.626 −23.882 −6.435 1.00 47.03 C ATOM 3699 O GLY D 113 50.533 −23.830 −5.852 1.00 47.41 O ATOM 3700 N GLU D 114 52.319 −25.001 −6.599 1.00 47.97 N ATOM 3701 CA GLU D 114 51.835 −26.273 −6.122 1.00 48.98 C ATOM 3702 CB GLU D 114 51.275 −27.062 −7.304 1.00 49.06 C ATOM 3703 CG GLU D 114 50.539 −28.280 −6.942 1.00 52.21 C ATOM 3704 CD GLU D 114 49.046 −28.083 −6.856 1.00 56.29 C ATOM 3705 OE1 GLU D 114 48.457 −28.646 −5.897 1.00 58.05 O ATOM 3706 OE2 GLU D 114 48.462 −27.412 −7.753 1.00 57.66 O ATOM 3707 C GLU D 114 52.968 −27.042 −5.375 1.00 49.12 C ATOM 3708 O GLU D 114 54.066 −27.250 −5.899 1.00 48.87 O ATOM 3709 N LYS D 115 52.678 −27.446 −4.147 1.00 48.78 N ATOM 3710 CA LYS D 115 53.615 −28.192 −3.317 1.00 48.72 C ATOM 3711 CB LYS D 115 53.481 −27.719 −1.866 1.00 49.82 C ATOM 3712 CG LYS D 115 54.298 −26.510 −1.509 1.00 51.17 C ATOM 3713 CD LYS D 115 54.010 −26.041 −0.090 1.00 56.06 C ATOM 3714 CE LYS D 115 55.030 −24.958 0.334 1.00 62.44 C ATOM 3715 NZ LYS D 115 54.544 −24.084 1.479 1.00 66.54 N ATOM 3716 C LYS D 115 53.450 −29.733 −3.408 1.00 47.04 C ATOM 3717 O LYS D 115 52.334 −30.258 −3.557 1.00 46.88 O ATOM 3718 N GLY D 116 54.576 −30.441 −3.346 1.00 46.00 N ATOM 3719 CA GLY D 116 54.576 −31.909 −3.157 1.00 44.67 C ATOM 3720 C GLY D 116 54.109 −32.255 −1.746 1.00 44.37 C ATOM 3721 O GLY D 116 54.088 −31.386 −0.850 1.00 44.53 O ATOM 3722 N ALA D 117 53.718 −33.515 −1.544 1.00 43.07 N ATOM 3723 CA ALA D 117 53.148 −33.918 −0.289 1.00 41.97 C ATOM 3724 CB ALA D 117 52.397 −35.199 −0.448 1.00 41.67 C ATOM 3725 C ALA D 117 54.208 −34.037 0.806 1.00 41.59 C ATOM 3726 O ALA D 117 53.855 −34.218 1.958 1.00 42.73 O ATOM 3727 N GLY D 118 55.487 −33.984 0.449 1.00 40.27 N ATOM 3728 CA GLY D 118 56.542 −33.997 1.430 1.00 39.78 C ATOM 3729 C GLY D 118 57.349 −35.274 1.452 1.00 41.03 C ATOM 3730 O GLY D 118 56.891 −36.346 1.032 1.00 41.30 O ATOM 3731 N THR D 119 58.575 −35.170 1.943 1.00 41.33 N ATOM 3732 CA THR D 119 59.336 −36.361 2.271 1.00 41.15 C ATOM 3733 CB THR D 119 60.404 −36.914 1.152 1.00 41.78 C ATOM 3734 OG1 THR D 119 61.763 −36.991 1.623 1.00 46.65 O ATOM 3735 CG2 THR D 119 60.283 −36.324 −0.201 1.00 36.84 C ATOM 3736 C THR D 119 59.867 −36.263 3.698 1.00 40.96 C ATOM 3737 O THR D 119 60.532 −35.282 4.053 1.00 40.91 O ATOM 3738 N ALA D 120 59.514 −37.258 4.517 1.00 38.25 N ATOM 3739 CA ALA D 120 60.005 −37.311 5.887 1.00 37.80 C ATOM 3740 CB ALA D 120 58.969 −38.040 6.791 1.00 35.79 C ATOM 3741 C ALA D 120 61.369 −38.034 5.933 1.00 37.39 C ATOM 3742 O ALA D 120 61.421 −39.245 5.827 1.00 37.29 O ATOM 3743 N LEU D 121 62.471 −37.298 6.048 1.00 37.88 N ATOM 3744 CA LEU D 121 63.791 −37.950 6.023 1.00 37.30 C ATOM 3745 CB LEU D 121 64.792 −37.133 5.216 1.00 37.16 C ATOM 3746 CG LEU D 121 66.302 −37.438 5.387 1.00 36.66 C ATOM 3747 CD1 LEU D 121 66.766 −38.702 4.727 1.00 34.65 C ATOM 3748 CD2 LEU D 121 67.118 −36.308 4.863 1.00 34.00 C ATOM 3749 C LEU D 121 64.286 −38.098 7.456 1.00 38.21 C ATOM 3750 O LEU D 121 64.305 −37.112 8.182 1.00 37.52 O ATOM 3751 N THR D 122 64.672 −39.322 7.853 1.00 39.39 N ATOM 3752 CA THR D 122 65.420 −39.553 9.093 1.00 40.36 C ATOM 3753 CB THR D 122 64.764 −40.661 9.897 1.00 41.03 C ATOM 3754 OG1 THR D 122 63.433 −40.254 10.264 1.00 40.03 O ATOM 3755 CG2 THR D 122 65.574 −41.056 11.168 1.00 41.88 C ATOM 3756 C THR D 122 66.850 −39.909 8.706 1.00 41.03 C ATOM 3757 O THR D 122 67.056 −40.848 7.985 1.00 40.84 O ATOM 3758 N VAL D 123 67.835 −39.101 9.103 1.00 42.99 N ATOM 3759 CA VAL D 123 69.234 −39.583 9.052 1.00 44.79 C ATOM 3760 CB VAL D 123 70.202 −38.754 8.099 1.00 45.22 C ATOM 3761 CG1 VAL D 123 71.523 −38.462 8.713 1.00 44.87 C ATOM 3762 CG2 VAL D 123 69.528 −37.548 7.456 1.00 43.50 C ATOM 3763 C VAL D 123 69.796 −40.080 10.409 1.00 46.99 C ATOM 3764 O VAL D 123 69.848 −39.349 11.408 1.00 46.54 O ATOM 3765 N LYS D 124 70.123 −41.378 10.437 1.00 49.38 N ATOM 3766 CA LYS D 124 70.636 −42.039 11.647 1.00 50.47 C ATOM 3767 CB LYS D 124 70.156 −43.525 11.743 1.00 49.98 C ATOM 3768 CG LYS D 124 68.619 −43.748 12.007 1.00 50.05 C ATOM 3769 CD LYS D 124 68.052 −43.043 13.279 1.00 49.05 C ATOM 3770 CE LYS D 124 66.688 −43.609 13.767 1.00 48.44 C ATOM 3771 NZ LYS D 124 65.834 −42.572 14.515 1.00 47.51 N ATOM 3772 C LYS D 124 72.171 −41.904 11.655 1.00 50.68 C ATOM 3773 O LYS D 124 72.808 −42.063 10.610 1.00 51.52 O ATOM 3774 N ALA D 125 72.722 −41.535 12.816 1.00 51.34 N ATOM 3775 CA ALA D 125 74.161 −41.416 13.055 1.00 52.01 C ATOM 3776 CB ALA D 125 74.443 −41.064 14.528 1.00 51.75 C ATOM 3777 C ALA D 125 74.834 −42.715 12.711 1.00 52.46 C ATOM 3778 O ALA D 125 74.540 −43.751 13.329 1.00 52.80 O ATOM 3779 OXT ALA D 125 75.650 −42.744 11.792 1.00 52.94 O ATOM 3780 O HOH W 1 27.537 −6.895 −25.418 1.00 49.96 O ATOM 3781 O HOH W 2 16.484 −15.501 −2.860 1.00 51.92 O ATOM 3782 O HOH W 3 64.994 −13.128 −29.648 1.00 61.47 O ATOM 3783 O HOH W 4 58.640 −8.263 −15.036 1.00 51.01 O ATOM 3784 O HOH W 5 49.811 −21.870 −19.181 1.00 53.77 O ATOM 3785 O HOH W 6 47.451 15.219 8.922 1.00 53.13 O ATOM 3786 O HOH W 7 57.241 6.450 −33.199 1.00 67.49 O ATOM 3787 O HOH W 8 55.602 −37.210 4.291 1.00 45.54 O ATOM 3788 O HOH W 9 71.793 −8.853 −14.510 1.00 53.04 O ATOM 3789 O HOH W 10 28.959 18.294 23.084 1.00 44.15 O ATOM 3790 O HOH W 11 51.211 −1.996 −16.782 1.00 34.13 O ATOM 3791 O HOH W 12 20.537 2.113 13.747 1.00 37.57 O ATOM 3792 O HOH W 13 63.618 −7.963 −22.008 1.00 48.46 O ATOM 3793 O HOH W 14 15.973 −5.480 −1.302 1.00 58.45 O ATOM 3794 O HOH W 15 47.026 19.336 −8.349 1.00 45.60 O ATOM 3795 O HOH W 16 38.870 18.600 16.145 1.00 48.41 O ATOM 3796 O HOH W 17 55.643 −13.712 −15.385 1.00 53.69 O ATOM 3797 O HOH W 18 29.523 17.221 14.352 1.00 33.22 O ATOM 3798 O HOH W 19 74.183 −13.852 −32.153 1.00 45.21 O ATOM 3799 O HOH W 20 51.603 5.048 −41.486 1.00 67.11 O ATOM 3800 O HOH W 21 75.638 −22.627 9.738 1.00 66.50 O ATOM 3801 O HOH W 22 16.178 1.770 −16.784 1.00 63.18 O ATOM 3802 O HOH W 23 72.855 −27.072 5.746 1.00 46.62 O ATOM 3803 O HOH W 24 28.469 17.946 −7.226 1.00 50.63 O ATOM 3804 O HOH W 25 52.814 15.053 −42.546 1.00 68.81 O ATOM 3805 O HOH W 26 54.094 10.191 −35.541 1.00 68.73 O ATOM 3806 O HOH W 27 28.221 15.502 −7.510 1.00 61.71 O ATOM 3807 O HOH W 28 29.651 −7.408 −0.031 1.00 77.42 O ATOM 3808 O HOH W 29 55.208 −11.816 −1.694 1.00 65.92 O ATOM 3809 O HOH W 30 65.842 −14.431 −7.424 1.00 62.18 O ATOM 3810 O HOH W 31 86.092 −37.988 19.084 1.00 62.21 O ATOM 3811 O HOH W 32 57.547 −17.020 −8.281 1.00 54.14 O ATOM 3812 O HOH W 33 15.238 −25.319 −14.960 1.00 48.17 O ATOM 3813 O HOH W 34 32.868 −10.730 −16.000 1.00 60.24 O ATOM 3814 O HOH W 35 27.383 −23.747 −14.732 1.00 54.01 O ATOM 3815 O HOH W 36 45.466 −36.429 −7.768 1.00 61.01 O ATOM 3816 O HOH W 37 85.751 6.805 −23.803 1.00 63.72 O ATOM 3817 O HOH W 38 64.003 −17.550 −25.097 1.00 52.50 O ATOM 3818 O HOH W 39 18.054 10.470 11.460 1.00 31.24 O ATOM 3819 O HOH W 40 3.495 −9.168 −13.711 1.00 46.96 O ATOM 3820 O HOH W 41 41.882 −5.080 13.345 1.00 59.64 O ATOM 3821 O HOH W 42 53.605 −40.677 −18.373 1.00 65.41 O ATOM 3822 O HOH W 43 36.386 −1.428 −3.036 1.00 50.71 O ATOM 3823 O HOH W 44 73.455 −43.317 −0.552 1.00 59.07 O ATOM 3824 O HOH W 45 78.144 −43.753 12.847 1.00 65.80 O ATOM 3825 O HOH W 46 57.888 −11.778 −11.462 1.00 57.52 O ATOM 3826 O HOH W 47 45.202 −5.340 3.650 1.00 48.23 O ATOM 3827 O HOH W 48 63.611 −10.382 −24.415 1.00 50.05 O ATOM 3828 O HOH W 49 57.536 6.456 −7.141 1.00 28.46 O ATOM 3829 O HOH W 50 58.272 −0.505 −0.424 1.00 30.38 O ATOM 3830 O HOH W 51 46.690 −1.769 0.708 1.00 25.84 O ATOM 3831 O HOH W 52 43.295 5.650 −15.284 1.00 31.89 O ATOM 3832 O HOH W 53 64.526 9.634 −19.506 1.00 29.96 O ATOM 3833 O HOH W 54 23.155 −22.622 −14.253 1.00 34.18 O ATOM 3834 O HOH W 55 64.074 −2.755 −3.506 1.00 32.46 O ATOM 3835 O HOH W 56 65.733 −39.979 14.780 1.00 50.48 O ATOM 3836 O HOH W 57 25.603 12.096 6.016 1.00 29.23 O ATOM 3837 O HOH W 58 16.263 −22.766 −25.732 1.00 37.53 O ATOM 3838 O HOH W 59 51.239 2.681 −2.880 1.00 34.06 O ATOM 3839 O HOH W 60 54.458 −2.187 −19.524 1.00 40.20 O ATOM 3840 O HOH W 61 71.361 7.864 −19.372 1.00 37.66 O ATOM 3841 O HOH W 62 56.520 7.752 −18.350 1.00 37.39 O ATOM 3842 O HOH W 63 13.694 −9.946 −29.896 1.00 38.42 O ATOM 3843 O HOH W 64 61.439 −41.245 8.021 1.00 41.37 O ATOM 3844 O HOH W 65 39.971 3.043 13.470 1.00 51.30 O ATOM 3845 O HOH W 66 28.958 15.268 1.059 1.00 43.67 O ATOM 3846 O HOH W 67 30.104 2.750 2.608 1.00 40.29 O ATOM 3847 O HOH W 68 69.821 −2.267 −8.072 1.00 33.11 O ATOM 3848 O HOH W 69 52.286 −7.121 −16.541 1.00 38.11 O ATOM 3849 O HOH W 70 58.487 −28.442 5.036 1.00 37.01 O ATOM 3850 O HOH W 71 25.719 16.565 13.085 1.00 44.30 O ATOM 3851 O HOH W 72 52.822 −11.013 −17.837 1.00 45.81 O ATOM 3852 O HOH W 73 22.805 −12.848 −21.485 1.00 48.51 O ATOM 3853 O HOH W 74 36.702 17.554 5.981 1.00 37.50 O ATOM 3854 O HOH W 75 71.895 −9.443 −24.558 1.00 45.80 O ATOM 3855 O HOH W 76 41.108 15.717 −5.487 1.00 39.02 O ATOM 3856 O HOH W 77 18.799 8.481 10.303 1.00 46.57 O ATOM 3857 O HOH W 78 61.610 7.007 −4.915 1.00 50.08 O ATOM 3858 O HOH W 79 60.439 −0.706 −2.323 1.00 33.12 O ATOM 3859 O HOH W 80 58.416 5.614 −9.104 1.00 39.99 O ATOM 3860 O HOH W 81 55.764 −3.255 −35.605 1.00 54.28 O ATOM 3861 O HOH W 82 42.688 13.409 7.580 1.00 32.60 O ATOM 3862 O HOH W 83 56.203 7.504 −13.473 1.00 53.50 O ATOM 3863 O HOH W 84 49.392 −17.628 −1.745 1.00 48.43 O ATOM 3864 O HOH W 85 38.478 17.991 −4.303 1.00 51.79 O ATOM 3865 O HOH W 86 27.380 11.533 −6.035 1.00 43.44 O ATOM 3866 O HOH W 87 17.419 −2.527 −17.186 1.00 46.81 O ATOM 3867 O HOH W 88 65.605 11.412 −34.743 1.00 39.99 O ATOM 3868 O HOH W 89 22.567 −9.323 0.874 1.00 67.08 O ATOM 3869 O HOH W 90 60.466 −7.608 −10.787 1.00 44.79 O ATOM 3870 O HOH W 91 70.029 13.354 −25.195 1.00 48.65 O ATOM 3871 O HOH W 92 27.738 −0.724 12.598 1.00 46.67 O ATOM 3872 O HOH W 93 67.709 −9.736 −34.668 1.00 44.52 O ATOM 3873 O HOH W 94 66.469 −42.220 −2.677 1.00 50.32 O ATOM 3874 O HOH W 95 39.659 4.264 19.635 1.00 47.26 O ATOM 3875 O HOH W 96 33.798 −0.629 0.634 1.00 57.82 O ATOM 3876 O HOH W 97 68.516 5.533 −7.794 1.00 38.76 O ATOM 3877 O HOH W 98 57.378 4.251 −27.603 1.00 49.36 O ATOM 3878 O HOH W 99 45.738 12.067 6.077 1.00 40.86 O ATOM 3879 O HOH W 100 72.260 −27.692 −8.666 1.00 69.19 O ATOM 3880 O HOH W 101 74.870 5.332 −30.099 1.00 41.86 O ATOM 3881 O HOH W 102 19.884 −13.568 −28.826 1.00 38.32 O ATOM 3882 O HOH W 103 3.023 −14.597 −13.318 1.00 47.56 O ATOM 3883 O HOH W 104 44.498 −8.083 −17.403 1.00 48.70 O ATOM 3884 O HOH W 105 75.836 −5.431 −10.641 1.00 58.00 O ATOM 3885 O HOH W 106 60.710 7.924 −15.560 1.00 30.19 O ATOM 3886 O HOH W 107 40.439 −9.476 15.038 1.00 60.28 O ATOM 3887 O HOH W 108 56.235 −30.734 8.744 1.00 53.65 O ATOM 3888 O HOH W 109 63.101 −1.697 −1.511 1.00 31.65 O ATOM 3889 O HOH W 110 56.808 5.705 −16.251 1.00 33.23 O ATOM 3890 O HOH W 111 38.263 8.376 22.049 1.00 55.72 O ATOM 3891 O HOH W 112 64.897 −23.439 −3.286 1.00 46.93 O ATOM 3892 O HOH W 113 30.449 −20.129 −16.647 1.00 51.12 O ATOM 3893 O HOH W 114 24.716 −6.274 −13.423 1.00 48.87 O ATOM 3894 O HOH W 115 69.646 14.058 −27.887 1.00 43.33 O ATOM 3895 O HOH W 116 74.378 8.019 −23.439 1.00 42.12 O ATOM 3896 O HOH W 117 74.411 −6.755 −12.312 1.00 46.21 O ATOM 3897 O HOH W 118 80.776 −40.223 6.131 1.00 51.98 O ATOM 3898 O HOH W 119 16.271 −26.835 −20.387 1.00 53.48 O ATOM 3899 O HOH W 120 45.888 8.444 12.000 1.00 56.59 O ATOM 3900 O HOH W 121 69.004 −39.355 13.718 1.00 48.52 O ATOM 3901 O HOH W 122 44.628 1.826 3.253 1.00 55.53 O ATOM 3902 O HOH W 123 10.540 −21.289 −24.117 1.00 55.75 O ATOM 3903 O HOH W 124 39.519 7.553 −11.796 1.00 42.99 O ATOM 3904 O HOH W 125 17.953 2.631 6.934 1.00 46.87 O ATOM 3905 O HOH W 126 59.706 −42.276 8.568 1.00 49.22 O ATOM 3906 O HOH W 127 71.515 9.604 −9.652 1.00 51.76 O ATOM 3907 O HOH W 128 22.711 −2.131 7.099 1.00 56.06 O ATOM 3908 O HOH W 129 50.497 1.860 −26.962 1.00 48.49 O ATOM 3909 O HOH W 130 13.213 −25.189 −17.571 1.00 47.33 O ATOM 3910 O HOH W 131 36.422 −18.594 1.861 1.00 59.55 O ATOM 3911 O HOH W 132 67.824 −18.443 8.774 1.00 64.42 O ATOM 3912 O HOH W 133 38.702 9.149 25.860 1.00 63.04 O ATOM 3913 O HOH W 134 26.829 −19.030 −19.104 1.00 49.31 O ATOM 3914 O HOH W 135 59.736 −32.012 10.576 1.00 35.03 O ATOM 3915 O HOH W 136 64.103 0.614 −0.340 1.00 40.32 O ATOM 3916 O HOH W 137 68.933 −33.671 −8.563 1.00 47.24 O ATOM 3917 O HOH W 138 30.091 −18.545 3.715 1.00 65.55 O ATOM 3918 O HOH W 139 11.871 −19.774 −24.246 1.00 33.50 O ATOM 3919 O HOH W 140 54.104 −8.838 −17.264 1.00 43.66 O ATOM 3920 O HOH W 141 68.475 −6.296 −7.780 1.00 51.54 O ATOM 3921 O HOH W 142 61.319 8.970 −35.221 1.00 63.08 O ATOM 3922 O HOH W 143 5.216 −2.074 −13.989 1.00 53.77 O ATOM 3923 O HOH W 144 77.471 −7.485 −20.605 1.00 62.28 O ATOM 3924 O HOH W 145 22.942 −15.078 −26.211 1.00 45.04 O ATOM 3925 O HOH W 146 62.912 −3.121 −6.057 1.00 35.08 O ATOM 3926 O HOH W 147 60.466 −10.624 −21.327 1.00 50.25 O ATOM 3927 O HOH W 148 49.218 8.905 −16.800 1.00 51.16 O ATOM 3928 O HOH W 149 33.265 10.047 −10.678 1.00 48.18 O ATOM 3929 O HOH W 150 58.095 9.361 −4.575 1.00 50.70 O ATOM 3930 O HOH W 151 44.991 −5.664 −19.770 1.00 52.37 O ATOM 3931 O HOH W 152 46.997 −10.249 −1.900 1.00 46.25 O ATOM 3932 O HOH W 153 30.534 2.664 −1.760 1.00 51.90 O ATOM 3933 O HOH W 154 75.688 −26.530 1.235 1.00 61.29 O ATOM 3934 O HOH W 155 31.837 18.468 15.789 1.00 47.11 O ATOM 3935 O HOH W 156 22.573 −6.055 −12.416 1.00 40.78 O ATOM 3936 O HOH W 157 69.966 −24.619 2.582 1.00 51.01 O ATOM 3937 O HOH W 158 7.080 −14.929 −10.596 1.00 46.45 O ATOM 3938 O HOH W 159 30.087 19.609 −1.446 1.00 65.48 O ATOM 3939 O HOH W 160 35.321 18.508 20.566 1.00 53.81 O ATOM 3940 O HOH W 161 66.872 −33.922 14.718 1.00 52.80 O ATOM 3941 O HOH W 162 19.048 −21.457 −21.483 1.00 49.57 O ATOM 3942 O HOH W 163 55.940 2.690 −8.893 1.00 32.16 O ATOM 3943 O HOH W 164 73.832 −5.186 −31.071 1.00 44.92 O ATOM 3944 O HOH W 165 73.497 4.469 −51.566 1.00 49.98 O ATOM 3945 O HOH W 166 46.143 −24.184 2.265 1.00 65.14 O ATOM 3946 O HOH W 167 53.822 −6.318 −27.868 1.00 59.13 O ATOM 3947 O HOH W 168 22.273 −7.060 −32.842 1.00 55.91 O ATOM 3948 O HOH W 169 69.920 5.647 −54.927 1.00 52.38 O ATOM 3949 O HOH W 170 75.276 −0.500 −18.493 1.00 56.03 O ATOM 3950 O HOH W 171 74.355 −7.796 −18.378 1.00 51.15 O ATOM 3951 O HOH W 172 49.846 7.730 −10.950 1.00 26.02 O ATOM 3952 O HOH W 173 74.688 6.874 −18.930 1.00 59.05 O ATOM 3953 O HOH W 174 8.532 −17.930 −12.696 1.00 46.51 O ATOM 3954 O HOH W 175 65.329 10.399 −23.289 1.00 31.68 O ATOM 3955 O HOH W 176 62.448 −6.262 −23.487 1.00 45.41 O ATOM 3956 O HOH W 177 13.206 −11.211 −6.299 1.00 49.50 O ATOM 3957 O HOH W 178 61.714 2.022 −1.453 1.00 36.23 O ATOM 3958 O HOH W 179 46.778 11.434 −6.992 1.00 35.69 O ATOM 3959 O HOH W 180 27.754 6.719 −4.382 1.00 58.45 O ATOM 3960 O HOH W 181 15.241 −0.832 −13.316 1.00 42.58 O ATOM 3961 O HOH W 182 58.699 9.096 −7.863 1.00 34.47 O ATOM 3962 O HOH W 183 64.941 −16.861 0.001 1.00 64.80 O ATOM 3963 O HOH W 184 77.519 −7.298 −17.771 1.00 59.86 O ATOM 3964 O HOH W 185 61.404 −45.244 5.009 1.00 47.15 O ATOM 3965 O HOH W 186 21.672 −2.040 −10.318 1.00 50.64 O ATOM 3966 O HOH W 187 29.956 −0.092 −9.945 1.00 62.76 O ATOM 3967 O HOH W 188 36.410 15.705 −10.591 1.00 55.05 O ATOM 3968 O HOH W 189 77.269 −24.718 −6.307 1.00 58.93 O ATOM 3969 O HOH W 190 53.639 −41.684 4.960 1.00 46.88 O ATOM 3970 O HOH W 191 39.701 −8.194 −19.650 1.00 68.65 O ATOM 3971 O HOH W 192 72.960 11.333 −30.255 1.00 57.07 O ATOM 3972 O HOH W 193 69.245 −8.902 −20.463 1.00 59.91 O ATOM 3973 O HOH W 194 25.519 2.766 −5.298 1.00 62.24 O ATOM 3974 O HOH W 195 23.823 −18.240 −23.523 1.00 53.83 O ATOM 3975 O HOH W 196 76.411 −10.927 −28.761 1.00 57.41 O ATOM 3976 O HOH W 197 68.909 7.633 −3.751 1.00 54.97 O ATOM 3977 O HOH W 198 68.238 4.063 −57.802 1.00 60.28 O ATOM 3978 O HOH W 199 57.902 −43.905 0.785 1.00 47.08 O ATOM 3979 O HOH W 200 26.387 1.586 19.253 1.00 57.98 O ATOM 3980 O HOH W 201 37.729 12.225 22.176 1.00 36.41 O ATOM 3981 O HOH W 202 52.534 7.353 −41.886 1.00 66.91 O ATOM 3982 O HOH W 203 27.054 −0.735 4.862 1.00 51.36 O ATOM 3983 O HOH W 204 42.236 −8.736 1.239 1.00 49.54 O ATOM 3984 O HOH W 205 72.453 −49.755 2.535 1.00 57.88 O ATOM 3985 O HOH W 206 21.715 13.751 27.357 1.00 63.70 O ATOM 3986 O HOH W 207 72.850 11.054 −33.545 1.00 48.23 O ATOM 3987 O HOH W 208 72.490 9.599 −53.823 1.00 63.34 O ATOM 3988 O HOH W 209 62.543 16.639 −24.176 1.00 32.72 O ATOM 3989 O HOH W 210 45.124 −6.604 −14.457 1.00 40.86 O ATOM 3990 O HOH W 211 67.128 11.703 −20.217 1.00 33.12 O ATOM 3991 O HOH W 212 71.826 −45.136 14.739 1.00 57.74 O ATOM 3992 O HOH W 213 57.710 7.585 −21.003 1.00 45.04 O ATOM 3993 O HOH W 214 38.961 −13.213 −15.679 1.00 47.33 O ATOM 3994 O HOH W 215 44.800 6.821 8.691 1.00 43.90 O ATOM 3995 O HOH W 216 52.098 −22.105 −2.209 1.00 58.29 O ATOM 3996 O HOH W 217 59.838 −5.952 −22.966 1.00 42.78 O ATOM 3997 O HOH W 218 18.495 −22.454 −8.937 1.00 43.08 O ATOM 3998 O HOH W 219 41.438 −0.960 2.947 1.00 47.12 O ATOM 3999 O HOH W 220 28.357 −12.574 2.320 1.00 67.42 O ATOM 4000 O HOH W 221 31.534 1.142 5.187 1.00 52.28 O ATOM 4001 O HOH W 222 52.061 −0.982 −33.448 1.00 66.10 O ATOM 4002 O HOH W 223 70.684 −25.967 −10.607 1.00 59.78 O ATOM 4003 O HOH W 224 24.630 −22.237 −21.050 1.00 62.09 O ATOM 4004 O HOH W 225 42.829 −4.753 −0.058 1.00 47.47 O ATOM 4005 O HOH W 226 70.534 13.938 −33.309 1.00 57.59 O ATOM 4006 O HOH W 227 37.629 6.169 −9.632 1.00 35.87 O ATOM 4007 O HOH W 228 39.050 −3.195 8.473 1.00 56.47 O ATOM 4008 O HOH W 229 50.163 −25.989 −2.653 1.00 57.19 O ATOM 4009 O HOH W 230 66.728 8.298 −2.609 1.00 53.22 O ATOM 4010 O HOH W 231 46.144 4.981 2.915 1.00 49.44 O ATOM 4011 O HOH W 232 64.030 15.931 −27.869 1.00 50.25 O ATOM 4012 O HOH W 233 78.237 −11.718 −16.675 1.00 66.40 O ATOM 4013 O HOH W 234 3.812 −6.905 −25.561 1.00 46.71 O ATOM 4014 O HOH W 235 64.296 −9.563 −18.956 1.00 55.82 O ATOM 4015 O HOH W 236 57.040 10.985 −10.979 1.00 33.38 O ATOM 4016 O HOH W 237 68.114 0.724 −44.435 1.00 47.88 O ATOM 4017 O HOH W 238 77.812 2.986 −35.556 1.00 54.12 O ATOM 4018 O HOH W 239 68.542 13.125 −10.000 1.00 42.93 O ATOM 4019 O HOH W 240 70.815 11.906 −8.762 1.00 61.18 O ATOM 4020 O HOH W 241 59.743 −4.943 −32.625 1.00 68.83 O ATOM 4021 O HOH W 242 53.599 −2.593 −24.738 1.00 57.17 O ATOM 4022 O HOH W 243 28.804 −22.157 −13.530 1.00 66.00 O ATOM 4023 O HOH W 244 12.528 −20.034 −9.931 1.00 54.81 O ATOM 4024 O HOH W 245 18.999 −13.928 −26.454 1.00 37.34 O ATOM 4025 O HOH W 246 9.399 −7.555 −10.236 1.00 51.74 O ATOM 4026 O HOH W 247 9.422 −23.577 −21.883 1.00 51.71 O ATOM 4027 O HOH W 248 48.989 16.285 −2.427 1.00 52.11 O ATOM 4028 O HOH W 249 25.370 13.160 27.839 1.00 51.67 O ATOM 4029 O HOH W 250 34.924 12.483 −8.217 1.00 36.25 O ATOM 4030 O HOH W 251 55.418 −37.562 −1.079 1.00 39.90 O ATOM 4031 O HOH W 252 65.053 −34.377 −13.229 1.00 61.20 O ATOM 4032 O HOH W 253 65.103 −23.855 −7.015 1.00 61.09 O ATOM 4033 O HOH W 254 59.191 −30.854 12.930 1.00 31.05 O ATOM 4034 O HOH W 255 74.576 −21.281 −5.297 1.00 62.37 O ATOM 4035 O HOH W 256 77.566 −33.129 5.274 1.00 55.66 O ATOM 4036 O HOH W 257 53.903 −22.288 −17.014 1.00 50.27 O ATOM 4037 O HOH W 258 45.037 −8.754 −15.227 1.00 49.48 O ATOM 4038 O HOH W 259 22.148 10.033 10.947 1.00 39.41 O ATOM 4039 O HOH W 260 65.185 −7.017 −20.794 1.00 45.24 O ATOM 4040 O HOH W 261 35.881 −2.206 17.490 1.00 44.28 O ATOM 4041 O HOH W 262 51.882 0.389 −39.836 1.00 67.72 O ATOM 4042 O HOH W 263 31.840 18.088 10.972 1.00 46.55 O ATOM 4043 O HOH W 264 0.515 −17.290 −27.161 1.00 54.35 O ATOM 4044 O HOH W 265 69.618 −46.411 15.204 1.00 62.11 O ATOM 4045 O HOH W 266 30.859 7.314 28.270 1.00 50.41 O ATOM 4046 O HOH W 267 18.081 11.850 9.552 1.00 53.90 O ATOM 4047 O HOH W 268 59.391 −23.586 16.532 1.00 66.97 O ATOM 4048 O HOH W 269 35.395 5.989 −11.309 1.00 48.68 O ATOM 4049 O HOH W 270 16.271 1.278 9.498 1.00 66.12 O ATOM 4050 O HOH W 271 46.429 19.602 7.510 1.00 50.45 O ATOM 4051 O HOH W 272 41.687 0.016 6.150 1.00 48.74 O ATOM 4052 O HOH W 273 55.497 −10.087 2.040 1.00 52.80 O ATOM 4053 O HOH W 274 11.272 −9.479 −30.539 1.00 38.85 O ATOM 4054 O HOH W 275 54.397 −1.130 −21.031 1.00 54.26 O ATOM 4055 O HOH W 276 12.883 −21.707 −24.390 1.00 53.71 O ATOM 4056 O HOH W 277 18.287 −21.975 −25.586 1.00 45.47 O ATOM 4057 O HOH W 278 46.785 0.418 −18.533 1.00 32.22 O ATOM 4058 O HOH W 279 45.873 −0.317 −20.312 1.00 58.31 O ATOM 4059 O HOH W 280 46.094 −1.639 −18.715 1.00 40.18 O ATOM 4060 O HOH W 281 42.337 −11.592 −18.551 1.00 65.25 O ATOM 4061 O HOH W 282 39.890 13.264 −12.839 1.00 51.77 O ATOM 4062 O HOH W 283 44.794 10.396 3.595 1.00 40.28 O ATOM 4063 O HOH W 284 39.618 18.733 13.341 1.00 51.45 O ATOM 4064 O HOH W 285 53.173 −35.468 −3.845 1.00 38.36 O ATOM 4065 O HOH W 286 17.906 −8.860 −0.520 1.00 47.10 O ATOM 4066 O HOH W 287 67.074 −7.604 −16.718 1.00 36.14 O ATOM 4067 O HOH W 288 12.354 −4.311 −22.662 1.00 46.21 O ATOM 4068 O HOH W 289 74.559 −22.448 −0.574 1.00 63.95 O ATOM 4069 O HOH W 290 24.579 9.857 −1.018 1.00 42.40 O ATOM 4070 O HOH W 291 42.836 −14.137 −19.076 1.00 48.67 O ATOM 4071 O HOH W 292 42.577 −32.888 −9.222 1.00 58.27 O ATOM 4072 O HOH W 293 51.889 −30.288 0.706 1.00 47.73 O ATOM 4073 O HOH W 294 58.591 9.524 −11.965 1.00 64.46 O ATOM 4074 O HOH W 295 23.195 6.118 25.651 1.00 51.90 O ATOM 4075 O HOH W 296 62.053 −7.731 −30.991 1.00 49.35 O ATOM 4076 O HOH W 297 49.685 −0.059 −34.867 1.00 57.45 O ATOM 4077 O HOH W 298 27.481 15.626 30.011 1.00 62.52 O ATOM 4078 O HOH W 299 22.412 16.454 25.493 1.00 43.70 O ATOM 4079 O HOH W 300 63.991 −24.156 −11.886 1.00 44.37 O ATOM 4080 O HOH W 301 23.584 −2.108 −14.137 1.00 51.53 O ATOM 4081 O HOH W 302 16.320 −11.014 1.961 1.00 61.11 O ATOM 4082 O HOH W 303 21.217 −22.569 −24.840 1.00 58.72 O ATOM 4083 O HOH W 304 41.646 17.848 −7.228 1.00 65.03 O ATOM 4084 O HOH W 305 22.950 17.731 10.015 1.00 58.75 O ATOM 4085 O HOH W 306 56.767 7.202 2.006 1.00 62.33 O ATOM 4086 O HOH W 307 58.177 −38.332 −8.428 1.00 51.10 O ATOM 4087 O HOH W 308 36.859 6.714 22.042 1.00 67.48 O ATOM 4088 O HOH W 309 8.548 −9.082 −6.377 1.00 64.08 O ATOM 4089 O HOH W 310 77.441 6.499 −18.901 1.00 53.22 O ATOM 4090 O HOH W 311 50.214 −2.598 −28.240 1.00 65.39 O ATOM 4091 O HOH W 312 67.157 −32.383 12.563 1.00 52.04 O ATOM 4092 O HOH W 313 42.103 10.501 15.691 1.00 58.68 O ATOM 4093 O HOH W 314 32.134 −22.541 −14.797 1.00 64.57 O ATOM 4094 O HOH W 315 49.067 3.344 −37.222 1.00 67.11 O ATOM 4095 O HOH W 316 61.987 −46.753 3.536 1.00 61.36 O ATOM 4096 O HOH W 317 60.318 −9.489 −9.294 1.00 50.74 O ATOM 4097 O HOH W 318 48.190 −10.315 0.317 1.00 44.60 O ATOM 4098 O HOH W 319 50.098 −10.842 −18.057 1.00 53.04 O ATOM 4099 O HOH W 320 46.094 9.952 6.886 1.00 54.78 O ATOM 4100 O HOH W 321 74.455 7.920 −30.461 1.00 54.66 O ATOM 4101 O HOH W 322 73.297 −11.177 −30.246 1.00 54.61 O ATOM 4102 O HOH W 323 55.869 3.785 −16.712 1.00 47.04 O ATOM 4103 O HOH W 324 17.752 −20.654 −6.176 1.00 66.30 O ATOM 4104 O HOH W 325 19.223 −5.198 −23.515 1.00 66.40 O ATOM 4105 O HOH W 326 14.416 −5.443 −29.063 1.00 58.70 O ATOM 4106 O HOH W 327 20.794 −20.150 −22.576 1.00 47.38 O ATOM 4107 O HOH W 328 46.970 9.591 −3.000 1.00 61.77 O ATOM 4108 O HOH W 329 44.733 9.137 −4.905 1.00 58.82 O ATOM 4109 O HOH W 330 44.656 15.089 8.206 1.00 62.37 O ATOM 4110 O HOH W 331 41.354 13.880 11.375 1.00 49.54 O ATOM 4111 O HOH W 332 37.483 14.530 22.480 1.00 53.31 O ATOM 4112 O HOH W 333 41.722 19.379 −3.546 1.00 50.97 O ATOM 4113 O HOH W 334 42.731 13.993 −12.884 1.00 72.77 O ATOM 4114 O HOH W 335 23.790 0.599 10.614 1.00 45.38 O ATOM 4115 O HOH W 336 59.513 −7.372 −13.143 1.00 61.55 O ATOM 4116 O HOH W 337 56.314 9.708 −14.663 1.00 50.95 O ATOM 4117 O HOH W 338 31.978 −18.528 −15.554 1.00 67.33 O ATOM 4118 O HOH W 339 56.351 −11.784 −4.728 1.00 42.25 O ATOM 4119 O HOH W 340 32.235 −7.490 −8.002 1.00 48.45 O ATOM 4120 O HOH W 341 11.039 −11.212 −5.888 1.00 56.05 O ATOM 4121 O HOH W 342 45.883 15.519 −9.499 1.00 60.90 O ATOM 4122 O HOH W 343 42.607 11.894 21.114 1.00 59.64 O ATOM 4123 O HOH W 344 64.897 −45.210 2.801 1.00 46.00 O ATOM 4124 O HOH W 345 62.414 −44.124 9.836 1.00 54.24 O ATOM 4125 O HOH W 346 66.607 −47.490 14.098 1.00 51.46 O ATOM 4126 O HOH W 347 33.184 9.901 29.054 1.00 54.19 O ATOM 4127 O HOH W 348 61.338 −8.260 −18.802 1.00 61.80 O ATOM 4128 O HOH W 349 58.915 10.462 −1.335 1.00 59.07 O ATOM 4129 O HOH W 350 72.985 11.119 −6.571 1.00 57.45 O ATOM 4130 O HOH W 351 52.715 −5.406 −30.681 1.00 76.01 O ATOM 4131 O HOH W 352 79.919 −27.316 −4.944 1.00 61.96 O ATOM 4132 O HOH W 353 71.264 8.651 −47.201 1.00 49.44 O ATOM 4133 O HOH W 354 22.664 12.842 33.813 1.00 49.23 O ATOM 4134 O HOH W 355 27.068 20.483 22.480 1.00 39.84 O ATOM 4135 O HOH W 356 31.821 −0.902 1.857 1.00 55.00 O ATOM 4136 O HOH W 357 35.021 −1.745 3.155 1.00 59.58 O ATOM 4137 O HOH W 358 39.467 2.391 21.237 1.00 73.05 O ATOM 4138 O HOH W 359 35.690 −6.904 −2.480 1.00 64.18 O ATOM 4139 O HOH W 360 38.038 −8.228 −14.500 1.00 64.77 O ATOM 4140 O HOH W 361 56.585 −29.520 5.841 1.00 60.72 O ATOM 4141 O HOH W 362 55.461 −35.538 5.382 1.00 54.96 O ATOM 4142 O HOH W 363 62.048 −20.002 −5.479 1.00 55.47 O ATOM 4143 O HOH W 364 65.219 −29.258 15.468 1.00 67.43 O ATOM 4144 O HOH W 365 15.338 −5.304 −5.505 1.00 54.06 O ATOM 4145 O HOH W 366 28.667 17.880 30.849 1.00 58.81 O ATOM 4146 O HOH W 367 7.490 −4.018 −9.949 1.00 49.82 O ATOM 4147 O HOH W 368 41.902 −0.891 15.421 1.00 58.16 O ATOM 4148 O HOH W 369 23.205 −24.145 −0.987 1.00 49.15 O ATOM 4149 O HOH W 370 46.687 7.432 6.640 1.00 58.62 O ATOM 4150 O HOH W 371 47.413 16.850 −8.082 1.00 59.32 O ATOM 4151 O HOH W 372 6.503 −2.107 −24.879 1.00 52.47 O ATOM 4152 O HOH W 373 47.592 −16.616 −26.050 1.00 54.23 O ATOM 4153 O HOH W 374 32.148 2.927 25.177 1.00 51.95 O ATOM 4154 O HOH W 375 70.869 13.479 −15.671 1.00 61.78 O ATOM 4155 O HOH W 376 32.233 −9.491 0.706 1.00 64.72 O ATOM 4156 O HOH W 377 43.162 −20.025 −20.830 1.00 61.56 O ATOM 4157 O HOH W 378 7.447 −21.877 −18.708 1.00 54.28 O ATOM 4158 O HOH W 379 64.478 −20.926 −14.628 1.00 56.28 O ATOM 4159 O HOH W 380 70.262 −45.646 1.731 1.00 65.26 O ATOM 4160 O HOH W 381 20.516 12.524 8.760 1.00 43.73 O ATOM 4161 O HOH W 382 74.928 8.949 −8.247 1.00 54.24 O ATOM 4162 O HOH W 383 18.257 −25.208 −7.910 1.00 50.96 O ATOM 4163 O HOH W 384 34.170 18.737 17.233 1.00 47.03 O ATOM 4164 O HOH W 385 21.137 2.084 3.808 1.00 65.70 O ATOM 4165 O HOH W 386 38.186 −4.444 −15.698 1.00 66.07 O ATOM 4166 O HOH W 387 38.985 −6.466 −8.831 1.00 51.93 O ATOM 4167 O HOH W 388 3.906 −16.558 −13.958 1.00 54.64 O ATOM 4168 O HOH W 389 33.087 −21.326 −9.095 1.00 66.75 O ATOM 4169 O HOH W 390 27.295 −14.177 5.542 1.00 58.06 O ATOM 4170 O HOH W 391 41.013 −5.818 20.816 1.00 60.46 O ATOM 4171 O HOH W 392 22.713 1.185 14.363 1.00 64.09 O ATOM 4172 O HOH W 393 48.064 6.165 1.998 1.00 61.05 O ATOM 4173 O HOH W 394 46.193 7.105 3.046 1.00 37.46 O 

1-23. (canceled)
 24. A compound for inhibiting, disrupting or detecting amyloid β-peptide oligomer formation or toxic activity, wherein the compound interacts with one or more amino acids 18-41 of the Ap protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.
 25. A compound as claimed in claim 24 wherein the compound interacts with the region of Aβ-peptide defined by N27, K28, I32 and L34 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.
 26. A compound as claimed in claim 24 wherein the compound interacts with the region of Aβ-peptide defined by F19, A21, G25, N27, K28, G29, I31, L34 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.
 27. A compound as claimed in claim 25 in which the compound is the peptide 27-NKGAI-31 to compete with formation of the dimer.
 28. A compound as claimed in claim 25 in which the compound is the peptide 27-NKxxIxxL-34 (wherein x is any amino acid).
 29. A compound as claimed in claim 24 in which the compound is an antibody or an antigen binding region thereof which binds Aβ-peptide in the region defined by N2′7, K28, I31 and L34.
 30. A compound as claimed in claim 24 in which the compound is an antibody or an antigen binding region thereof which binds Ap-peptide in the region defined by F19, A21, G25, N27, K28, G29, I31, L34.
 31. A compound as claimed in claim 24 wherein the compound interacts with the region of Aβ-peptide defined by G33, L34, M35 and V36 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.
 32. A compound as claimed in claim 24 wherein the compound interacts with the region of Aβ-peptide defined by I32, G33, L34, M35, V36 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.
 33. A compound as claimed in claim 31 in which the compound is the peptide 33-GLMV-36 to compete for tetramer with or without flanking residues,
 34. A compound as claimed in claim 31 in which the compound is the peptide 31-IIGLxV-36 (wherein x is any amino acid).
 35. A compound as claimed in claim 31 in which the compound is an antibody or an antigen binding region thereof which binds Ap-peptide in the region defined by G33, L34, M35 and V36.
 36. A compound as claimed in claim 32 in which the compound is an antibody or an antigen binding region thereof which binds Aβ-peptide in the region defined by I32, G33, L34, M35, V36.
 37. A compound as claimed in claim 24 wherein the compound interacts with the region of Ap-peptide defined by V18, F20, S26, K28, G29, I32, M35, V39 and I41 of Aβ-peptide wherein amino acids 18-41 of the Ap protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.
 38. A compound as claimed in claim 24 wherein the compound interacts with the region of Aβ-peptide defined by V18, F20, D23, S26, K28, A30, I32, M35, G37, V39, I41 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.
 39. A compound as claimed in claim 37 in which the compound is the peptide selected from the group consisting of the peptides 26-SxKG-29, 18-VxF-20, 32-IxxM-35, and 39-VxI-41 each with or without flanking sequences; wherein the peptide competes for formation of amyloid.
 40. A compound as claimed in claim 37 in which the compound is an antibody or an antigen binding region thereof which binds Aβ-peptide in the region defined by V18, F20, S26, K28, G29, I32, M35, V39 and I41.
 41. A compound as claimed in claim 38 in which the compound is an antibody or an antigen binding region thereof which binds A)₃-peptide in the region defined by V18, F20, D23, S26, K28, A30, I32, M35, G37, V39 and I41. 42-49. (canceled) 